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Conserved domains on  [gi|71986426|ref|NP_001024517|]
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Protein kinase C-like 2 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
351-673 0e+00

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 680.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05587 161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 591 GCTGDDEsasRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFS 670
Cdd:cd05587 241 GCGPTGE---RDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLVIMNIDQSEFEGFS 317

                ...
gi 71986426 671 FVN 673
Cdd:cd05587 318 FVN 320
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
161-291 1.03e-84

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


:

Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 262.20  E-value: 1.03e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 161 RGRLRIEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSgCKSKQKTKTLRATLNPQWNETFTYKLLPGDKD 240
Cdd:cd04026   1 RGRIYLKISVKDNKLTVEVREAKNLIPMDPNGLSDPYVKLKLIPDPK-NETKQKTKTIKKTLNPVWNETFTFDLKPADKD 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 241 RRLSIEVWDWDRTSRNDFMGSLSFGISELMKEAASGWYKLLSAEEGEFYNI 291
Cdd:cd04026  80 RRLSIEVWDWDRTTRNDFMGSLSFGVSELIKMPVDGWYKLLNQEEGEYYNV 130
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
37-94 2.16e-38

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410383  Cd Length: 58  Bit Score: 136.00  E-value: 2.16e-38
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426  37 KSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADKG 94
Cdd:cd20833   1 KDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCSFVVHKRCHEFVTFSCPGADKG 58
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
104-157 1.17e-37

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410386  Cd Length: 54  Bit Score: 133.62  E-value: 1.17e-37
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCGTDN 157
Cdd:cd20836   1 HKFKVHTYSSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKRCVKNVPSLCGTDH 54
 
Name Accession Description Interval E-value
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
351-673 0e+00

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 680.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05587 161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 591 GCTGDDEsasRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFS 670
Cdd:cd05587 241 GCGPTGE---RDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLVIMNIDQSEFEGFS 317

                ...
gi 71986426 671 FVN 673
Cdd:cd05587 318 FVN 320
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
348-609 6.45e-95

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.67  E-value: 6.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHP-NIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTKTF 507
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELFTAITEHNVSYP---KSLSKEAVSLCKALLI 583
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPppeWDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|....*.
gi 71986426    584 KNPSKRLGCtgddesasRDIKEHPFF 609
Cdd:smart00220 237 KDPEKRLTA--------EEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
344-669 7.40e-85

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 270.15  E-value: 7.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  344 KASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLY 423
Cdd:PTZ00263  16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHP-FIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnifgdAT 503
Cdd:PTZ00263  95 FLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  504 TKTF--CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKAL 581
Cdd:PTZ00263 170 DRTFtlCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  582 LIKNPSKRLGCTGDdesASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDhSFLKLPTKMTPPdwevLENL 661
Cdd:PTZ00263 250 LQTDHTKRLGTLKG---GVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-KYPDSPVDRLPP----LTAA 321

                 ....*...
gi 71986426  662 KGDEFSNF 669
Cdd:PTZ00263 322 QQAEFAGF 329
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
161-291 1.03e-84

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 262.20  E-value: 1.03e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 161 RGRLRIEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSgCKSKQKTKTLRATLNPQWNETFTYKLLPGDKD 240
Cdd:cd04026   1 RGRIYLKISVKDNKLTVEVREAKNLIPMDPNGLSDPYVKLKLIPDPK-NETKQKTKTIKKTLNPVWNETFTFDLKPADKD 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 241 RRLSIEVWDWDRTSRNDFMGSLSFGISELMKEAASGWYKLLSAEEGEFYNI 291
Cdd:cd04026  80 RRLSIEVWDWDRTTRNDFMGSLSFGVSELIKMPVDGWYKLLNQEEGEYYNV 130
Pkinase pfam00069
Protein kinase domain;
348-609 4.89e-59

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 197.85  E-value: 4.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDvECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHP-NIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLfflhskgiiyrdlkldnvmlERDGHikitdfgmckenifgdatTKTF 507
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGL--------------------ESGSS------------------LTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI---TEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIidqPYAFPELPSNLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|....*
gi 71986426   585 NPSKRLGCTgddesasrDIKEHPFF 609
Cdd:pfam00069 201 DPSKRLTAT--------QALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
353-589 3.28e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 3.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:COG0515  14 LLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPN-IVRVYDVGEEDGRPYLVMEYVEGE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT-TKTFCGTP 511
Cdd:COG0515  93 SLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTqTGTVVGTP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI--------TEHNVSYPKSLSKeavsLCKALLI 583
Cdd:COG0515 173 GYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHlrepppppSELRPDLPPALDA----IVLRALA 248

                ....*.
gi 71986426 584 KNPSKR 589
Cdd:COG0515 249 KDPEER 254
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
37-94 2.16e-38

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410383  Cd Length: 58  Bit Score: 136.00  E-value: 2.16e-38
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426  37 KSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADKG 94
Cdd:cd20833   1 KDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCSFVVHKRCHEFVTFSCPGADKG 58
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
104-157 1.17e-37

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 133.62  E-value: 1.17e-37
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCGTDN 157
Cdd:cd20836   1 HKFKVHTYSSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKRCVKNVPSLCGTDH 54
C2 pfam00168
C2 domain;
174-280 2.40e-33

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 123.20  E-value: 2.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIpedsGCKSKQKTKTLRATLNPQWNETFTYKlLPGDKDRRLSIEVWDWDRT 253
Cdd:pfam00168   2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLL----DGKQKKKTKVVKNTLNPVWNETFTFS-VPDPENAVLEIEVYDYDRF 76
                          90       100
                  ....*....|....*....|....*...
gi 71986426   254 SRNDFMGSLSFGISEL-MKEAASGWYKL 280
Cdd:pfam00168  77 GRDDFIGEVRIPLSELdSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
174-278 2.20e-29

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 112.20  E-value: 2.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDsgcKSKQKTKTLRATLNPQWNETFTYKLLPgDKDRRLSIEVWDWDRT 253
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDP---KEKKKTKVVKNTLNPVWNETFEFEVPP-PELAELEIEVYDKDRF 76
                           90       100
                   ....*....|....*....|....*
gi 71986426    254 SRNDFMGSLSFGISELMKEAASGWY 278
Cdd:smart00239  77 GRDDFIGQVTIPLSDLLLGGRHEKL 101
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
423-589 8.00e-23

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 102.95  E-value: 8.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGmckenI---F 499
Cdd:NF033483  83 YIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFG-----IaraL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  500 GDAT---TKTFCGTPDYIAPEiilyQPYGKSV----DWWAYGVLLFEMLAGQPPFDGED----------EDelFTAITEH 562
Cdd:NF033483 158 SSTTmtqTNSVLGTVHYLSPE----QARGGTVdarsDIYSLGIVLYEMLTGRPPFDGDSpvsvaykhvqED--PPPPSEL 231
                        170       180
                 ....*....|....*....|....*..
gi 71986426  563 NVSYPKSLskEAVSLcKAlLIKNPSKR 589
Cdd:NF033483 232 NPGIPQSL--DAVVL-KA-TAKDPDDR 254
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
39-91 5.63e-21

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 86.34  E-value: 5.63e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71986426    39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGA 91
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
104-154 5.94e-20

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 83.65  E-value: 5.94e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71986426   104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECG 51
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
39-88 4.43e-17

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 75.20  E-value: 4.43e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 71986426     39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
104-153 6.29e-16

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 72.12  E-value: 6.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 71986426    104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
175-297 4.05e-14

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 76.34  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  175 LTIKILEAKNLIPMDPNGLSDPYVKCKLipedsGCKSKQKTKTLRATLNPQWNETFTYKLLPGDKDrRLSIEVWDWDRTS 254
Cdd:COG5038 1042 LTIMLRSGENLPSSDENGYSDPFVKLFL-----NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKD-VLTINVNDWDSGE 1115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 71986426  255 RNDFMGSLSFGISELMKEAASGWYKLLSAEEGEFYNINITPEY 297
Cdd:COG5038 1116 KNDLLGTAEIDLSKLEPGGTTNSNIPLDGKTFIVLDGTLHPGF 1158
 
Name Accession Description Interval E-value
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
351-673 0e+00

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 680.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05587 161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 591 GCTGDDEsasRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFS 670
Cdd:cd05587 241 GCGPTGE---RDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLVIMNIDQSEFEGFS 317

                ...
gi 71986426 671 FVN 673
Cdd:cd05587 318 FVN 320
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
347-673 0e+00

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 586.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd05616  81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd05616 161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 587 SKRLGCTGDDEsasRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKtDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEF 666
Cdd:cd05616 241 GKRLGCGPEGE---RDIKEHAFFRYIDWEKLERKEIQPPYKPKAC-GRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEF 316

                ....*..
gi 71986426 667 SNFSFVN 673
Cdd:cd05616 317 EGFSFVN 323
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
353-672 0e+00

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 585.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05570   2 VLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05570  82 DLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05570 162 YIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLGC 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TGDDESasrDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFV 672
Cdd:cd05570 242 GPKGEA---DIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDSDLLTNIDQEEFRGFSYI 318
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
337-677 0e+00

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 547.67  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 337 SSNHNVIKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCF 416
Cdd:cd05615   1 SNNLDRVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd05615  81 QTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVS 576
Cdd:cd05615 161 HMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 577 LCKALLIKNPSKRLGCTGDDEsasRDIKEHPFFRRIDWFKIETRQIQPPFKPKLkTDRSTENFDHSFLKLPTKMTPPDWE 656
Cdd:cd05615 241 ICKGLMTKHPAKRLGCGPEGE---RDIREHAFFRRIDWDKLENREIQPPFKPKV-CGKGAENFDKFFTRGQPVLTPPDQL 316
                       330       340
                ....*....|....*....|.
gi 71986426 657 VLENLKGDEFSNFSFVNPFYV 677
Cdd:cd05615 317 VIANIDQADFEGFSYVNPQFV 337
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
353-673 2.24e-170

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 489.70  E-value: 2.24e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05591   2 VLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05591  82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05591 162 YIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLGC 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TGdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFV 672
Cdd:cd05591 242 VA-SQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQINQEEFRGFSFV 320

                .
gi 71986426 673 N 673
Cdd:cd05591 321 N 321
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
353-674 1.37e-169

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 487.66  E-value: 1.37e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05592   2 VLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05592  82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05592 162 YIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLGV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 tgdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFV 672
Cdd:cd05592 242 ---PECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPVDKKLLASMDQEQFKGFSFT 318

                ..
gi 71986426 673 NP 674
Cdd:cd05592 319 NP 320
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
353-674 5.60e-148

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 432.79  E-value: 5.60e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05590   2 VLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05590  82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05590 162 YIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLGS 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TgdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFV 672
Cdd:cd05590 242 L--TLGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEESLLPMINQDEFRNFSYT 319

                ..
gi 71986426 673 NP 674
Cdd:cd05590 320 AP 321
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
353-674 1.03e-143

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 421.66  E-value: 1.03e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05620   2 VLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05620  82 DLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGTPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05620 162 YIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLGV 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TGddesasrDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFV 672
Cdd:cd05620 242 VG-------NIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSYSDKNLIDSMDQSAFAGFSFI 314

                ..
gi 71986426 673 NP 674
Cdd:cd05620 315 NP 316
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
343-674 3.43e-143

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 420.87  E-value: 3.43e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRL 422
Cdd:cd05619   2 LTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDA 502
Cdd:cd05619  82 FFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALL 582
Cdd:cd05619 162 KTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLF 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 583 IKNPSKRLGCTGddesasrDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLK 662
Cdd:cd05619 242 VREPERRLGVRG-------DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMD 314
                       330
                ....*....|..
gi 71986426 663 GDEFSNFSFVNP 674
Cdd:cd05619 315 QNMFRNFSFVNP 326
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
353-674 2.47e-135

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 400.19  E-value: 2.47e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05571   2 VLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHP-FLTSLKYSFQTNDRLCFVMEYVNGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05571  81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05571 161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPD---WEVLENLKGDEFSNF 669
Cdd:cd05571 241 GPRD---AKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDrgdLLGLEEEERPHFEQF 317

                ....*
gi 71986426 670 SFVNP 674
Cdd:cd05571 318 SYSAS 322
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
352-672 3.91e-132

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 392.17  E-value: 3.91e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05588  81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFD--GED-------EDELFTAITEHNVSYPKSLSKEAVSLCKALL 582
Cdd:cd05588 161 NYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDivGSSdnpdqntEDYLFQVILEKPIRIPRSLSVKAASVLKGFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 583 IKNPSKRLGCtgDDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLK 662
Cdd:cd05588 241 NKNPAERLGC--HPQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPDDPDVIEKID 318
                       330
                ....*....|
gi 71986426 663 GDEFSNFSFV 672
Cdd:cd05588 319 QSEFEGFEYV 328
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
348-674 3.16e-131

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 389.74  E-value: 3.16e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPE--KPSFLVALHSCFQTMDRLYFV 425
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNsaRHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQvGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI-FGDaTT 504
Cdd:cd05589  81 MEYAAGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMgFGD-RT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:cd05589 159 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 585 NPSKRLGCTGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPP-DWEVLENLKG 663
Cdd:cd05589 239 NPERRLGASERD---AEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPkEPRPLTEEEQ 315
                       330
                ....*....|.
gi 71986426 664 DEFSNFSFVNP 674
Cdd:cd05589 316 ALFKDFDYVAD 326
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
354-609 1.47e-127

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: 377.63  E-value: 1.47e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHP-FIVKLHYAFQTEEKLYLVLDYVPGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPDY 513
Cdd:cd05123  80 LFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 514 IAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGCT 593
Cdd:cd05123 160 LAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG 239
                       250
                ....*....|....*.
gi 71986426 594 GDDEsasrdIKEHPFF 609
Cdd:cd05123 240 GAEE-----IKAHPFF 250
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
352-647 3.46e-117

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 353.55  E-value: 3.46e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05575  81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLG 591
Cdd:cd05575 161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 592 CTGDdesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLP 647
Cdd:cd05575 241 SGND----FLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREP 292
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
347-681 3.32e-116

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 352.40  E-value: 3.32e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05617  16 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd05617  96 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTST 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF-------DGEDEDELFTAITEHNVSYPKSLSKEAVSLCK 579
Cdd:cd05617 176 FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEDYLFQVILEKPIRIPRFLSVKASHVLK 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 580 ALLIKNPSKRLGCtgDDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLE 659
Cdd:cd05617 256 GFLNKDPKERLGC--QPQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPVQLTPDDEDVIK 333
                       330       340
                ....*....|....*....|..
gi 71986426 660 NLKGDEFSNFSFVNPFYVKDVE 681
Cdd:cd05617 334 RIDQSEFEGFEYINPLLLSTEE 355
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
346-640 2.63e-113

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 342.25  E-value: 2.63e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHP-FIVNLLGSFQDDRNLYMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeniFGDATTK 505
Cdd:cd05580  80 MEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAK---RVKDRTY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKN 585
Cdd:cd05580 157 TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVD 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 586 PSKRLGCtgdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05580 237 LTKRLGN---LKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
347-681 7.88e-111

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 338.93  E-value: 7.88e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05618  21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd05618 101 EYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF---------DGEDEDELFTAITEHNVSYPKSLSKEAVSL 577
Cdd:cd05618 181 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnpDQNTEDYLFQVILEKQIRIPRSLSVKAASV 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 578 CKALLIKNPSKRLGCTgdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEV 657
Cdd:cd05618 261 LKSFLNKDPKERLGCH--PQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDI 338
                       330       340
                ....*....|....*....|....
gi 71986426 658 LENLKGDEFSNFSFVNPFYVKDVE 681
Cdd:cd05618 339 VRKIDQSEFEGFEYINPLLMSAEE 362
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
353-671 2.76e-110

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 336.21  E-value: 2.76e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05595   2 LLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHP-FLTALKYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05595  81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05595 161 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPD-WEVLENLKGDE---FSN 668
Cdd:cd05595 241 GPSD---AKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDrYDSLDLLESDQrthFPQ 317

                ...
gi 71986426 669 FSF 671
Cdd:cd05595 318 FSY 320
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
351-674 2.00e-108

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 331.29  E-value: 2.00e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKE---LFAIKVLKKDVIIQDD-DVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKTTGSDkgkIFAMKVLKKASIVRNQkDTAHTKAERNILEAVKHP-FIVDLHYAFQTGGKLYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd05584  80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd05584 160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 587 SKRLGCTGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFlklpTKMTP---PDWEVLENLKG 663
Cdd:cd05584 240 SSRLGSGPGD---AEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKF----TKQTPvdsPDDSTLSESAN 312
                       330
                ....*....|.
gi 71986426 664 DEFSNFSFVNP 674
Cdd:cd05584 313 QVFQGFTYVAP 323
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
337-671 8.54e-102

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 315.10  E-value: 8.54e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 337 SSNHNVIKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCF 416
Cdd:cd05593   6 TTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHP-FLTSLKYSF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd05593  85 QTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVS 576
Cdd:cd05593 165 GITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKS 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 577 LCKALLIKNPSKRLGCTGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPD-- 654
Cdd:cd05593 245 LLSGLLIKDPNKRLGGGPDD---AKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEky 321
                       330       340
                ....*....|....*....|.
gi 71986426 655 ----WEVLENLKGDEFSNFSF 671
Cdd:cd05593 322 dedgMDCMDNERRPHFPQFSY 342
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
343-674 4.05e-101

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 313.50  E-value: 4.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRL 422
Cdd:cd05594  22 VTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHP-FLTALKYSFQTHDRL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHS-KGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGD 501
Cdd:cd05594 101 CFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKAL 581
Cdd:cd05594 181 ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGL 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 582 LIKNPSKRLGCTGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDW----EV 657
Cdd:cd05594 261 LKKDPKQRLGGGPDD---AKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQMITITPPDQddsmET 337
                       330
                ....*....|....*..
gi 71986426 658 LENLKGDEFSNFSFVNP 674
Cdd:cd05594 338 VDNERRPHFPQFSYSAS 354
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
351-674 1.70e-98

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 305.73  E-value: 1.70e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd05604  81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05604 161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 591 GCTGDdesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFlklpTKMTPP------------DWEVL 658
Cdd:cd05604 241 GAKED----FLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEF----TEEMVPysvcvssdysivNASVL 312
                       330
                ....*....|....*.
gi 71986426 659 EnlKGDEFSNFSFVNP 674
Cdd:cd05604 313 E--ADDAFVGFSYAPP 326
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
353-672 1.84e-95

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 297.39  E-value: 1.84e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKE---LFAIKVLKKDVIIQDDDVECTMtEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFV 429
Cdd:cd05582   2 VLGQGSFGKVFLVRKITGPDagtLYAMKVLKKATLKVRDRVRTKM-ERDILADVNHP-FIVKLHYAFQTEGKLYLILDFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd05582  80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05582 160 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANR 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 590 LGCTGDdesASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFlklpTKMTPPDWEVLENLKGDE--FS 667
Cdd:cd05582 240 LGAGPD---GVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEF----TSRTPKDSPGVPPSANAHqlFR 312

                ....*
gi 71986426 668 NFSFV 672
Cdd:cd05582 313 GFSFV 317
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
348-609 6.45e-95

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.67  E-value: 6.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHP-NIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTKTF 507
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELFTAITEHNVSYP---KSLSKEAVSLCKALLI 583
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPppeWDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|....*.
gi 71986426    584 KNPSKRLGCtgddesasRDIKEHPFF 609
Cdd:smart00220 237 KDPEKRLTA--------EEALQHPFF 254
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
344-674 9.32e-95

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 296.54  E-value: 9.32e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 344 KASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLY 423
Cdd:cd05602   5 KPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd05602  85 FVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLI 583
Cdd:cd05602 165 TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQ 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 584 KNPSKRLGCTGDdesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTK----MTPPDWEVLE 659
Cdd:cd05602 245 KDRTKRLGAKDD----FTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPVPnsigQSPDSILVTA 320
                       330
                ....*....|....*..
gi 71986426 660 NLK--GDEFSNFSFVNP 674
Cdd:cd05602 321 SIKeaAEAFLGFSYAPP 337
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
353-672 2.45e-93

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 291.87  E-value: 2.45e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05603   2 VIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05603  82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTPE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05603 162 YLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLGA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 593 TGDdesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLK--LPTKMT-PPDWEVLENLKGDEFSNF 669
Cdd:cd05603 242 KAD----FLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQeaVPHSVGrTPDLTASSSSSSSAFLGF 317

                ...
gi 71986426 670 SFV 672
Cdd:cd05603 318 SYA 320
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
356-614 3.12e-93

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: 289.89  E-value: 3.12e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 356 KGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGDLM 435
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNP-FVVKLYYSFQGKKNLYLVMEYLPGGDLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 436 YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG---------------MCKENIFG 500
Cdd:cd05579  82 SLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGlskvglvrrqiklsiQKKSNGAP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK--SLSKEAVSLC 578
Cdd:cd05579 162 EKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKDLI 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 579 KALLIKNPSKRLGCTGDDEsasrdIKEHPFFRRIDW 614
Cdd:cd05579 242 SKLLTPDPEKRLGAKGIEE-----IKNHPFFKGIDW 272
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
353-671 6.09e-91

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 285.62  E-value: 6.09e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCP-FIVPLKFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLGC 592
Cdd:cd05585 160 YLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGY 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 593 TGDDEsasrdIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSF 671
Cdd:cd05585 240 NGAQE-----IKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSVVDDSHLSESVQQQFEGWSY 313
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
346-671 1.28e-90

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: 286.10  E-value: 1.28e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSP-WIVRLHYAFQDEDHLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK---------- 495
Cdd:cd05573  80 MEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTkmnksgdres 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 -------------ENIFGDATTKTF------CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELF 556
Cdd:cd05573 160 ylndsvntlfqdnVLARRRPHKQRRvraysaVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETY 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 557 TAITEHNVS--YPKS--LSKEAVSLCKALLIkNPSKRLGctgddesASRDIKEHPFFRRIDWFKIetRQIQPPFKPKLKT 632
Cdd:cd05573 240 SKIMNWKESlvFPDDpdVSPEAIDLIRRLLC-DPEDRLG-------SAEEIKAHPFFKGIDWENL--RESPPPFVPELSS 309
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 71986426 633 DRSTENFDH-SFLKLPTKMTPPDWEVLENLKGDEFSNFSF 671
Cdd:cd05573 310 PTDTSNFDDfEDDLLLSEYLSNGSPLLGKGKQLAFVGFTF 349
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
347-640 1.46e-90

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 283.53  E-value: 1.46e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd14209   2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFP-FLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifgDATTKT 506
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV---KGRTWT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14209 158 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 587 SKRLgctGDDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd14209 238 TKRF---GNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFD 288
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
346-609 2.85e-87

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: 274.48  E-value: 2.85e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHP-GIVKLYYTFQDESKLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--------EN 497
Cdd:cd05581  80 LEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdsspES 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IFGDATTK---------TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK 568
Cdd:cd05581 160 TKGDADSQiaynqaraaSFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71986426 569 SLSKEAVSLCKALLIKNPSKRLGCtgDDESASRDIKEHPFF 609
Cdd:cd05581 240 NFPPDAKDLIQKLLVLDPSKRLGV--NENGGYDELKAHPFF 278
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
346-630 4.45e-85

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: 270.26  E-value: 4.45e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHP-FLPTLYASFQTSTHLCFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDL--MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK-------- 495
Cdd:cd05574  80 MDYCPGGELfrLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtppp 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 -----------------ENIF----GDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDE 554
Cdd:cd05574 160 vrkslrkgsrrssvksiEKETfvaePSARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDE 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 555 LFTAITEHNVSYPKS--LSKEAVSLCKALLIKNPSKRLGCtgddESASRDIKEHPFFRRIDWFKIetRQIQPPFKPKL 630
Cdd:cd05574 240 TFSNILKKELTFPESppVSSEAKDLIRKLLVKDPSKRLGS----KRGASEIKRHPFFRGVNWALI--RNMTPPIIPRP 311
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
344-669 7.40e-85

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 270.15  E-value: 7.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  344 KASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLY 423
Cdd:PTZ00263  16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHP-FIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnifgdAT 503
Cdd:PTZ00263  95 FLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK-----VP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  504 TKTF--CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKAL 581
Cdd:PTZ00263 170 DRTFtlCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  582 LIKNPSKRLGCTGDdesASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDhSFLKLPTKMTPPdwevLENL 661
Cdd:PTZ00263 250 LQTDHTKRLGTLKG---GVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-KYPDSPVDRLPP----LTAA 321

                 ....*...
gi 71986426  662 KGDEFSNF 669
Cdd:PTZ00263 322 QQAEFAGF 329
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
161-291 1.03e-84

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 262.20  E-value: 1.03e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 161 RGRLRIEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSgCKSKQKTKTLRATLNPQWNETFTYKLLPGDKD 240
Cdd:cd04026   1 RGRIYLKISVKDNKLTVEVREAKNLIPMDPNGLSDPYVKLKLIPDPK-NETKQKTKTIKKTLNPVWNETFTFDLKPADKD 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 241 RRLSIEVWDWDRTSRNDFMGSLSFGISELMKEAASGWYKLLSAEEGEFYNI 291
Cdd:cd04026  80 RRLSIEVWDWDRTTRNDFMGSLSFGVSELIKMPVDGWYKLLNQEEGEYYNV 130
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
347-674 1.81e-84

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 269.48  E-value: 1.81e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKT---TKELFAIKVLKKDVIIQDDD-VECTMTEKRVLALPEKPSFLVALHSCFQTMDRL 422
Cdd:cd05614   1 NFELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRKAALVQKAKtVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDA 502
Cdd:cd05614  81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 T-TKTFCGTPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDE----DELFTAITEHNVSYPKSLSKEAVS 576
Cdd:cd05614 161 ErTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGEkntqSEVSRRILKCDPPFPSFIGPVARD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 577 LCKALLIKNPSKRLGCTgddESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKL-----PTKmT 651
Cdd:cd05614 241 LLQKLLCKDPKKRLGAG---PQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLepvysPAG-T 316
                       330       340
                ....*....|....*....|...
gi 71986426 652 PPDWEVLenlkgdeFSNFSFVNP 674
Cdd:cd05614 317 PPSGARV-------FQGYSFIAP 332
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
354-643 4.87e-83

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 265.59  E-value: 4.87e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVL---ALPEKPsFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESP-FIVGLKFSFQTPTDLYLVTDYMS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd05586  80 GGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS-LSKEAVSLCKALLIKNPSK 588
Cdd:cd05586 160 TEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDvLSDEGRSFVKGLLNRNPKH 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 589 RLGCTGDdesaSRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSF 643
Cdd:cd05586 240 RLGAHDD----AVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEF 290
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
353-612 9.42e-83

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 262.33  E-value: 9.42e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKT---TKELFAIKVLKKDVIIQDDDV-ECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd05583   1 VLGTGAYGKVFLVRKVGghdAGKLYAMKVLKKATIVQKAKTaEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG-DATTKTF 507
Cdd:cd05583  81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGeNDRAYSF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYG--KSVDWWAYGVLLFEMLAGQPPFDGEDED----ELFTAITEHNVSYPKSLSKEAVSLCKAL 581
Cdd:cd05583 161 CGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGERnsqsEISKRILKSHPPIPKTFSAEAKDFILKL 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 71986426 582 LIKNPSKRLGCTGDDesaSRDIKEHPFFRRI 612
Cdd:cd05583 241 LEKDPKKRLGAGPRG---AHEIKEHPFFKGL 268
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
346-640 6.88e-82

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


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 261.22  E-value: 6.88e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHP-FIIRLFWTEHDQRFLYML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIfgdATTK 505
Cdd:cd05612  80 MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR---DRTW 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKN 585
Cdd:cd05612 157 TLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVD 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 586 PSKRLGCTGDdesASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05612 237 RTRRLGNMKN---GADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFD 288
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
346-671 2.87e-77

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 250.31  E-value: 2.87e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05598   1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNE-WVVKLYYSFQDKENLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-----KENifg 500
Cdd:cd05598  80 MDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwTHD--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 datTKTFC-----GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDElftaiTEHNV-SYPKSL---- 570
Cdd:cd05598 157 ---SKYYLahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAE-----TQLKViNWRTTLkiph 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 571 ----SKEAVSLCKAlLIKNPSKRLGCTGDDEsasrdIKEHPFFRRIDWFKieTRQIQPPFKPKLKTDRSTENFD----HS 642
Cdd:cd05598 229 eanlSPEAKDLILR-LCCDAEDRLGRNGADE-----IKAHPFFAGIDWEK--LRKQKAPYIPTIRHPTDTSNFDpvdpEK 300
                       330       340
                ....*....|....*....|....*....
gi 71986426 643 FLKLPTKMTPPDWEVLENLKGDEFSNFSF 671
Cdd:cd05598 301 LRSSDEEPTTPNDPDNGKHPEHAFYEFTF 329
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
346-671 5.67e-77

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: 249.45  E-value: 5.67e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNP-WVVKLYYSFQDEENLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK---ENIFGDA 502
Cdd:cd05599  80 MEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTglkKSHLAYS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTktfcGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT--EHNVSYPK--SLSKEAVSLC 578
Cdd:cd05599 160 TV----GTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 579 KALLIkNPSKRLGCTGDDEsasrdIKEHPFFRRIDWFKIetRQIQPPFKPKLKTDRSTENFDH---SFLKLPTKMTPPDW 655
Cdd:cd05599 236 ERLLC-DAEHRLGANGVEE-----IKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFDEfeeVDLQIPSSPEAGKD 307
                       330
                ....*....|....*.
gi 71986426 656 EVLENLKGDEFSNFSF 671
Cdd:cd05599 308 SKELKSKDWVFIGYTY 323
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
354-628 6.45e-76

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 245.13  E-value: 6.45e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSP-FIVSLAYAFETKDKLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTKTFCGTP 511
Cdd:cd05577  80 LKYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVGTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQ-PYGKSVDWWAYGVLLFEMLAGQPPF----DGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd05577 159 GYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrqrkEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71986426 587 SKRLGCTGddeSASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05577 239 ERRLGCRG---GSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
354-614 1.57e-75

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 243.29  E-value: 1.57e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSP-FIVKLYRTFKDKKYLYMLMEYCLGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTKTFCGTPDY 513
Cdd:cd05572  80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTPEY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 514 IAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED--ELFTAITEHN--VSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05572 159 VAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGIdkIEFPKYIDKNAKNLIKQLLRRNPEER 238
                       250       260
                ....*....|....*....|....*
gi 71986426 590 LGCTgddESASRDIKEHPFFRRIDW 614
Cdd:cd05572 239 LGYL---KGGIRDIKKHKWFEGFDW 260
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
347-628 2.17e-75

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 244.14  E-value: 2.17e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKT---TKELFAIKVLKKDVIIQD-DDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRL 422
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLKKATIVQKaKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDA 502
Cdd:cd05613  81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKE-FLLDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTK--TFCGTPDYIAPEIILYQPYG--KSVDWWAYGVLLFEMLAGQPPF--DGED--EDELFTAITEHNVSYPKSLSKEA 574
Cdd:cd05613 160 NERaySFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFtvDGEKnsQAEISRRILKSEPPYPQEMSALA 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 575 VSLCKALLIKNPSKRLGCTGDDesaSRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05613 240 KDIIQRLLMKDPKKRLGCGPNG---ADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
347-608 3.33e-74

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: 239.34  E-value: 3.33e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKI-KREIEIMKLLNHP-NIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTKT 506
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-FRGGSLLKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKN 585
Cdd:cd14003 158 FCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVD 237
                       250       260
                ....*....|....*....|...
gi 71986426 586 PSKRLGCTgddesasrDIKEHPF 608
Cdd:cd14003 238 PSKRITIE--------EILNHPW 252
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
348-609 6.07e-74

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 239.08  E-value: 6.07e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHP-FLVNLWYSFQDEEDMYMVVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTf 507
Cdd:cd05578  81 LLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATST- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDG---EDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:cd05578 160 SGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIhsrTSIEEIRAKFETASVLYPAGWSEEAIDLINKLLER 239
                       250       260
                ....*....|....*....|....*
gi 71986426 585 NPSKRLGCtgddesaSRDIKEHPFF 609
Cdd:cd05578 240 DPQKRLGD-------LSDLKNHPYF 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
347-610 3.41e-73

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


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 236.60  E-value: 3.41e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPN-ILRLYGYFEDKKRIYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGdaTTKT 506
Cdd:cd14007  80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSN--RRKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14007 158 FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDP 237
                       250       260
                ....*....|....*....|....
gi 71986426 587 SKRLGCTgddesasrDIKEHPFFR 610
Cdd:cd14007 238 SKRLSLE--------QVLNHPWIK 253
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
347-614 5.30e-73

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: 237.30  E-value: 5.30e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENP-FVVSMYCSFETKRHLCMVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT--- 503
Cdd:cd05609  80 EYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTnly 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 -------TKTF-----CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS-- 569
Cdd:cd05609 160 eghiekdTREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGdd 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71986426 570 -LSKEAVSLCKALLIKNPSKRLGCTGddesaSRDIKEHPFFRRIDW 614
Cdd:cd05609 240 aLPDDAQDLITRLLQQNPLERLGTGG-----AEEVKQHPFFQDLDW 280
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
347-608 1.27e-72

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: 235.45  E-value: 1.27e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDvECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE-EMLRREIEILKRLDHPN-IVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENIFGDaT 503
Cdd:cd05117  79 ELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGE-K 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCK 579
Cdd:cd05117 158 LKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLIK 237
                       250       260
                ....*....|....*....|....*....
gi 71986426 580 ALLIKNPSKRLgctgddeSASrDIKEHPF 608
Cdd:cd05117 238 RLLVVDPKKRL-------TAA-EALNHPW 258
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
356-614 1.68e-72

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: 235.45  E-value: 1.68e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 356 KGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGDLM 435
Cdd:cd05611   6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 436 YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMcKENIFGDATTKTFCGTPDYIA 515
Cdd:cd05611  86 SLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL-SRNGLEKRHNKKFVGTPDYLA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 516 PEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK----SLSKEAVSLCKALLIKNPSKRLG 591
Cdd:cd05611 165 PETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEevkeFCSPEAVDLINRLLCMDPAKRLG 244
                       250       260
                ....*....|....*....|...
gi 71986426 592 CTGDDEsasrdIKEHPFFRRIDW 614
Cdd:cd05611 245 ANGYQE-----IKSHPFFKSINW 262
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
346-677 6.35e-71

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: 233.36  E-value: 6.35e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSP-WITKLQYAFQDSENLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG-MCKENIFGDAT 503
Cdd:cd05601  80 MEYHPGGDLLSLLsRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGsAAKLSSDKTVT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILY------QPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH--NVSYP--KSLSKE 573
Cdd:cd05601 160 SKMPVGTPDYIAPEVLTSmnggskGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFkkFLKFPedPKVSES 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 574 AVSLCKALLiKNPSKRLGCTGddesasrdIKEHPFFRRIDWFKIetRQIQPPFKPKLKTDRSTENFDhSFLKlptKMTPP 653
Cdd:cd05601 240 AVDLIKGLL-TDAKERLGYEG--------LCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFD-EFEP---KKTRP 304
                       330       340
                ....*....|....*....|....*.
gi 71986426 654 DWEvlENLKGDEFS--NFSFVNPFYV 677
Cdd:cd05601 305 SYE--NFNKSKGFSgkDLPFVGFTFT 328
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
353-628 1.01e-69

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 228.78  E-value: 1.01e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLalpEK--PSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05605   7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQIL---EKvnSRFVVSLAYAYETKDALCLVLTIMN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDaTTKTFC 508
Cdd:cd05605  84 GGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGE-TIRGRV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE----DELFTAITEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:cd05605 163 GTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYSEKFSEEAKSICSQLLQK 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71986426 585 NPSKRLGCtgdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05605 243 DPKTRLGC---RGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
353-628 3.24e-69

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 227.60  E-value: 3.24e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLalpEK--PSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd05630   7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQIL---EKvnSRFVVSLAYAYETKDALCLVLTLMN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeNIFGDATTKTFC 508
Cdd:cd05630  84 GGDLKFHIYHMGQagFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAV-HVPEGQTIKGRV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE----DELFTAITEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:cd05630 163 GTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKkikrEEVERLVKEVPEEYSEKFSPQARSLCSMLLCK 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71986426 585 NPSKRLGCTGddeSASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05630 243 DPAERLGCRG---GGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
353-628 4.78e-68

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 224.38  E-value: 4.78e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKpSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05608   8 VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHS-RFIVSLAYAFQTKTDLCLVMTIMNGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFC 508
Cdd:cd05608  87 DLRYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF--DGE--DEDELFTAITEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:cd05608 167 GTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFraRGEkvENKELKQRILNDSVTYSEKFSPASKSICEALLAK 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71986426 585 NPSKRLGCTgddESASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05608 247 DPEKRLGFR---DGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
348-628 2.29e-67

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 222.56  E-value: 2.29e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLalpEK--PSFLVALHSCFQTMDRLYFV 425
Cdd:cd05631   2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRIL---EKvnSRFVVSLAYAYETKDALCLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDaT 503
Cdd:cd05631  79 LTIMNGGDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGE-T 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE----DELFTAITEHNVSYPKSLSKEAVSLCK 579
Cdd:cd05631 158 VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEKFSEDAKSICR 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71986426 580 ALLIKNPSKRLGCTGddeSASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05631 238 MLLTKNPKERLGCRG---NGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
343-640 2.55e-66

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: 222.25  E-value: 2.55e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRL 422
Cdd:cd05596  23 MNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSE-WIVQLHYAFQDDKYL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-KENIFGD 501
Cdd:cd05596 102 YMVMDYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmKMDKDGL 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTFCGTPDYIAPEIILYQP----YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH--NVSYPK--SLSKE 573
Cdd:cd05596 181 VRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHknSLQFPDdvEISKD 260
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 574 AVSLCKALLIkNPSKRLGCTGDDEsasrdIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05596 261 AKSLICAFLT-DREVRLGRNGIEE-----IKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFD 321
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
346-640 1.02e-65

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: 219.91  E-value: 1.02e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd05597   1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRR-WITKLHYAFQDENYLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-KENIFGDAT 503
Cdd:cd05597  80 MDYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClKLREDGTVQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIIL-----YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH--NVSYPKS---LSKE 573
Cdd:cd05597 160 SSVAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHkeHFSFPDDeddVSEE 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 574 AVSLCKAlLIKNPSKRLGCTGDDesasrDIKEHPFFRRIDWFKIetRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05597 240 AKDLIRR-LICSRERRLGQNGID-----DFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFD 298
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
343-640 1.19e-65

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: 221.44  E-value: 1.19e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRL 422
Cdd:cd05600   8 LKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSP-WLVKLLYAFQDPENV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK------- 495
Cdd:cd05600  87 YLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkk 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 --------ENIFGDATT----------------------KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQP 545
Cdd:cd05600 167 iesmkirlEEVKNTAFLeltakerrniyramrkedqnyaNSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFP 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 546 PFDGEDEDELFTAIT--EHNVSYPK--------SLSKEAVSLCKaLLIKNPSKRLGCTgddesasRDIKEHPFFRRIDWF 615
Cdd:cd05600 247 PFSGSTPNETWANLYhwKKTLQRPVytdpdlefNLSDEAWDLIT-KLITDPQDRLQSP-------EQIKNHPFFKNIDWD 318
                       330       340
                ....*....|....*....|....*
gi 71986426 616 KIETrQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05600 319 RLRE-GSKPPFIPELESEIDTSYFD 342
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
347-640 1.96e-65

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: 219.75  E-value: 1.96e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd05610   5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSP-FIVHLYYSLQSANNVYLVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI-------- 498
Cdd:cd05610  84 EYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLnrelnmmd 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 -----------------------------FGDAT----------------TKTFCGTPDYIAPEIILYQPYGKSVDWWAY 533
Cdd:cd05610 164 ilttpsmakpkndysrtpgqvlslisslgFNTPTpyrtpksvrrgaarveGERILGTPDYLAPELLLGKPHGPAVDWWAL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 534 GVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP---KSLSKEAVSLCKALLIKNPSKRLGctgddesaSRDIKEHPFFR 610
Cdd:cd05610 244 GVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAG--------LKELKQHPLFH 315
                       330       340       350
                ....*....|....*....|....*....|
gi 71986426 611 RIDWFKIETRqiQPPFKPKLKTDRSTENFD 640
Cdd:cd05610 316 GVDWENLQNQ--TMPFIPQPDDETDTSYFE 343
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
347-639 6.76e-64

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: 216.64  E-value: 6.76e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd05629   2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSP-WVVSLYYSFQDAQYLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC------------ 494
Cdd:cd05629  81 EFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsayy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 ------KENIFGDATTKTF-----------------------------CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFE 539
Cdd:cd05629 161 qkllqgKSNKNRIDNRNSVavdsinltmsskdqiatwkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 540 MLAGQPPFDGEDEDELFTAIT--EHNVSYPK--SLSKEAVSLCKAlLIKNPSKRLGCTGDDEsasrdIKEHPFFRRIDWF 615
Cdd:cd05629 241 CLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRR-LITNAENRLGRGGAHE-----IKSHPFFRGVDWD 314
                       330       340
                ....*....|....*....|....
gi 71986426 616 KIetRQIQPPFKPKLKTDRSTENF 639
Cdd:cd05629 315 TI--RQIRAPFIPQLKSITDTSYF 336
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
348-628 1.41e-62

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 210.98  E-value: 1.41e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLalpEK--PSFLVALHSCFQTMDRLYFV 425
Cdd:cd05632   4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQIL---EKvnSQFVVNLAYAYETKDALCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDaT 503
Cdd:cd05632  81 LTIMNGGDLKFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGE-S 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE----DELFTAITEHNVSYPKSLSKEAVSLCK 579
Cdd:cd05632 160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICK 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71986426 580 ALLIKNPSKRLGCtgdDESASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05632 240 MLLTKDPKQRLGC---QEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
341-640 1.42e-62

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 211.76  E-value: 1.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  341 NVIKASDFNFLTVLGKGSFGKVLLGEQKTTK-ELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTM 419
Cdd:PTZ00426  25 NKMKYEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINHP-FCVNLYGSFKDE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  420 DRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeniF 499
Cdd:PTZ00426 104 SYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK---V 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  500 GDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCK 579
Cdd:PTZ00426 181 VDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMK 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426  580 ALLIKNPSKRLgctGDDESASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:PTZ00426 261 KLLSHDLTKRY---GNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
Pkinase pfam00069
Protein kinase domain;
348-609 4.89e-59

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 197.85  E-value: 4.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDvECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKD-KNILREIKILKKLNHP-NIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLfflhskgiiyrdlkldnvmlERDGHikitdfgmckenifgdatTKTF 507
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGL--------------------ESGSS------------------LTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI---TEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIidqPYAFPELPSNLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|....*
gi 71986426   585 NPSKRLGCTgddesasrDIKEHPFF 609
Cdd:pfam00069 201 DPSKRLTAT--------QALQHPWF 217
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
347-589 6.72e-59

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: 199.23  E-value: 6.72e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEA-LNEVKLLSKLKHP-NIVKYYESFEENGKLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDA 502
Cdd:cd08215  79 EYADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITehNVSY---PKSLSKEAVSLCK 579
Cdd:cd08215 159 LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIV--KGQYppiPSQYSSELRDLVN 236
                       250
                ....*....|
gi 71986426 580 ALLIKNPSKR 589
Cdd:cd08215 237 SMLQKDPEKR 246
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
347-608 1.56e-58

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: 198.01  E-value: 1.56e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPN-IVELHEVMATKTKIFFVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC--KENIFGDATT 504
Cdd:cd14663  80 ELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDGLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLI 583
Cdd:cd14663 160 HTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILD 239
                       250       260
                ....*....|....*....|....*
gi 71986426 584 KNPSKRLGCTGddesasrdIKEHPF 608
Cdd:cd14663 240 PNPSTRITVEQ--------IMASPW 256
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
343-640 6.04e-58

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 200.61  E-value: 6.04e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRL 422
Cdd:cd05621  49 MKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP-WVVQLFCAFQDDKYL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-KENIFGD 501
Cdd:cd05621 128 YMVMEYMPGGDLV-NLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCmKMDETGM 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTFCGTPDYIAPEIILYQP----YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH--NVSYPK--SLSKE 573
Cdd:cd05621 207 VHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHknSLNFPDdvEISKH 286
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 574 AVSLCKALLiKNPSKRLGCTGDDEsasrdIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05621 287 AKNLICAFL-TDREVRLGRNGVEE-----IKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFD 347
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
353-628 1.18e-57

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 196.50  E-value: 1.18e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLAL---PEKPSFLVALHSCFQTMDRLYFVMEFV 429
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDATTKTFCG 509
Cdd:cd05606  81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACD--FSKKKPHASVG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILY-QPYGKSVDWWAYGVLLFEMLAGQPPF---DGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKN 585
Cdd:cd05606 159 THGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRD 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71986426 586 PSKRLGCTGddeSASRDIKEHPFFRRIDWFKIETRQIQPPFKP 628
Cdd:cd05606 239 VSKRLGCLG---RGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
297-640 6.53e-57

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: 198.69  E-value: 6.53e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 297 YDEDMEKVRKKMN-ENFITR-DNSSSKPKDPAaprastlplgssnhnvIKASDFNFLTVLGKGSFGKVLLGEQKTTKELF 374
Cdd:cd05622  38 YDLDFPALRKNKNiDNFLSRyKDTINKIRDLR----------------MKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVY 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 375 AIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGDLMYQIQQVgKFKEPVAVFYAA 454
Cdd:cd05622 102 AMKLLSKFEMIKRSDSAFFWEERDIMAFANSP-WVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNY-DVPEKWARFYTA 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 455 EIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-KENIFGDATTKTFCGTPDYIAPEIILYQP----YGKSVD 529
Cdd:cd05622 180 EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECD 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 530 WWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH--NVSYPK--SLSKEAVSLCKALLiKNPSKRLGCTGDDEsasrdIKE 605
Cdd:cd05622 260 WWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHknSLTFPDdnDISKEAKNLICAFL-TDREVRLGRNGVEE-----IKR 333
                       330       340       350
                ....*....|....*....|....*....|....*
gi 71986426 606 HPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05622 334 HLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFD 368
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
347-653 1.47e-56

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: 197.92  E-value: 1.47e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLaLPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05624  73 DFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVL-VNGDCQWITTLHYAFQDENYLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-KENIFGDATT 504
Cdd:cd05624 152 DYYVGGDLLTLLSKFeDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSClKMNDDGTVQS 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQ-----PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHN-----VSYPKSLSKEA 574
Cdd:cd05624 232 SVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerfqfPSHVTDVSEEA 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 575 VSLCKAlLIKNPSKRLGCTGDDesasrDIKEHPFFRRIDWFKIetRQIQPPFKPKLKTDRSTENF--DHSFLKLPtKMTP 652
Cdd:cd05624 312 KDLIQR-LICSRERRLGQNGIE-----DFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFdvDDDVLRNP-EILP 382

                .
gi 71986426 653 P 653
Cdd:cd05624 383 P 383
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
346-640 1.49e-54

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 191.38  E-value: 1.49e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKpSFLVALHSCFQTMDRLYFV 425
Cdd:cd05626   1 SMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADN-EWVVKLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC----------- 494
Cdd:cd05626  80 MDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCtgfrwthnsky 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 ------------KENIFGDATTKTFC------------------------GTPDYIAPEIILYQPYGKSVDWWAYGVLLF 538
Cdd:cd05626 160 yqkgshirqdsmEPSDLWDDVSNCRCgdrlktleqratkqhqrclahslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 539 EMLAGQPPF--DGEDEDELFTAITEHNVSYPKS--LSKEAVSLCKALLIkNPSKRLGCTGDDesasrDIKEHPFFRRIDw 614
Cdd:cd05626 240 EMLVGQPPFlaPTPTETQLKVINWENTLHIPPQvkLSPEAVDLITKLCC-SAEERLGRNGAD-----DIKAHPFFSEVD- 312
                       330       340
                ....*....|....*....|....*.
gi 71986426 615 FKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05626 313 FSSDIRTQPAPYVPKISHPMDTSNFD 338
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
348-629 1.51e-54

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 188.57  E-value: 1.51e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd05607   4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSP-FIVSLAYAFETKTHLCLVMS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd05607  83 LMNGGDLKYHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TfCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF----DGEDEDELFTAITEHNVSYP-KSLSKEAVSLCKA 580
Cdd:cd05607 163 R-AGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrdhkEKVSKEELKRRTLEDEVKFEhQNFTEEAKDICRL 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71986426 581 LLIKNPSKRLGCTGDDEsasrDIKEHPFFRRIDWFKIETRQIQPPFKPK 629
Cdd:cd05607 242 FLAKKPENRLGSRTNDD----DPRKHEFFKSINFPRLEAGLIDPPFVPD 286
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
346-640 3.82e-54

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: 190.26  E-value: 3.82e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKpSFLVALHSCFQTMDRLYFV 425
Cdd:cd05625   1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADN-EWVVRLYYSFQDKDNLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK---------- 495
Cdd:cd05625  80 MDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdsky 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 --------------ENIFGDATT-----------------------KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLF 538
Cdd:cd05625 160 yqsgdhlrqdsmdfSNEWGDPENcrcgdrlkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 539 EMLAGQPPFDGEDEDELFTAI----TEHNVSYPKSLSKEAVSLCkALLIKNPSKRLGCTGDDEsasrdIKEHPFFRRIDw 614
Cdd:cd05625 240 EMLVGQPPFLAQTPLETQMKVinwqTSLHIPPQAKLSPEASDLI-IKLCRGPEDRLGKNGADE-----IKAHPFFKTID- 312
                       330       340
                ....*....|....*....|....*.
gi 71986426 615 FKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05625 313 FSSDLRQQSAPYIPKITHPTDTSNFD 338
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
354-591 1.58e-53

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: 184.35  E-value: 1.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKL-NKKLQENLESEIAILKSIKHPN-IVRLYDVQKTEDFIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGMCKeNIFGDATTKTFCGT 510
Cdd:cd14009  79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFAR-SLQPASMAETLCGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI--TEHNVSYP--KSLSKEAVSLCKALLIKNP 586
Cdd:cd14009 158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIerSDAVIPFPiaAQLSPDCKDLLRRLLRRDP 237

                ....*
gi 71986426 587 SKRLG 591
Cdd:cd14009 238 AERIS 242
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
354-609 1.92e-53

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: 184.68  E-value: 1.92e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQ------DDDVECTMTE--KRVLALPEK---PSfLVALHSCF--QTMD 420
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKrregknDRGKIKNALDdvRREIAIMKKldhPN-IVRLYEVIddPESD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGGDLMY--QIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI 498
Cdd:cd14008  80 KLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 FGDATTKTFCGTPDYIAPEI--ILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSY--PKSLSKE 573
Cdd:cd14008 160 DGNDTLQKTAGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFpiPPELSPE 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 574 AVSLCKALLIKNPSKRLGctgddesaSRDIKEHPFF 609
Cdd:cd14008 240 LKDLLRRMLEKDPEKRIT--------LKEIKEHPWV 267
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
354-607 2.74e-53

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: 182.47  E-value: 2.74e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLNHP-NIVKLYDVFETENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCG--T 510
Cdd:cd00180  78 LKdLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMlagqppfdgededelftaitehnvsypkslsKEAVSLCKALLIKNPSKRL 590
Cdd:cd00180 158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRP 206
                       250
                ....*....|....*..
gi 71986426 591 gctgddeSAsRDIKEHP 607
Cdd:cd00180 207 -------SA-KELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
353-589 2.82e-53

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: 183.94  E-value: 2.82e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14014   7 LLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPN-IVRVYDVGEDDGRPYIVMEYVEGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDAT---TKTFCG 509
Cdd:cd14014  86 SLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARA--LGDSGltqTGSVLG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV----SYPKSLSKEAVSLCKALLIKN 585
Cdd:cd14014 164 TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpppsPLNPDVPPALDAIILRALAKD 243

                ....
gi 71986426 586 PSKR 589
Cdd:cd14014 244 PEER 247
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
353-589 3.28e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 3.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:COG0515  14 LLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPN-IVRVYDVGEEDGRPYLVMEYVEGE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT-TKTFCGTP 511
Cdd:COG0515  93 SLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTqTGTVVGTP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI--------TEHNVSYPKSLSKeavsLCKALLI 583
Cdd:COG0515 173 GYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHlrepppppSELRPDLPPALDA----IVLRALA 248

                ....*.
gi 71986426 584 KNPSKR 589
Cdd:COG0515 249 KDPEER 254
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
347-653 4.06e-51

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: 182.91  E-value: 4.06e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKpSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05623  73 DFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDS-QWITTLHYAFQDDNNLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTK 505
Cdd:cd05623 152 DYYVGGDLLTLLSKFeDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLK-LMEDGTVQ 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 T--FCGTPDYIAPEIILYQP-----YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHN--VSYPKSL---SKE 573
Cdd:cd05623 231 SsvAVGTPDYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKerFQFPTQVtdvSEN 310
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 574 AVSLCKAlLIKNPSKRLGCTGDDesasrDIKEHPFFRRIDWFKIetRQIQPPFKPKLKTDRSTENF--DHSFLKLPTKMT 651
Cdd:cd05623 311 AKDLIRR-LICSREHRLGQNGIE-----DFKNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSNFdvDDDCLKNCETMP 382

                ..
gi 71986426 652 PP 653
Cdd:cd05623 383 PP 384
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
353-609 4.14e-51

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: 178.10  E-value: 4.14e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVlkkdVIIQDDD---VECTMTEKRVL-ALPEKpsFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd06606   7 LLGKGSFGSVYLALNLDTGELMAVKE----VELSGDSeeeLEALEREIRILsSLKHP--NIVRYLGTERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFGDATTKT 506
Cdd:cd06606  81 VPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFdgEDEDELFTAI-----TEHNVSYPKSLSKEAVSLCKAL 581
Cdd:cd06606 161 LRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW--SELGNPVAALfkigsSGEPPPIPEHLSEEAKDFLRKC 238
                       250       260
                ....*....|....*....|....*...
gi 71986426 582 LIKNPSKRLGCtgddesasRDIKEHPFF 609
Cdd:cd06606 239 LQRDPKKRPTA--------DELLQHPFL 258
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
347-640 1.17e-50

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 179.09  E-value: 1.17e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPS--FLVALHSCFQTMDRLYF 424
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDcpFIVCMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDATT 504
Cdd:cd14223  81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACD--FSKKKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQ-PYGKSVDWWAYGVLLFEMLAGQPPF---DGEDEDELFTAITEHNVSYPKSLSKEAVSLCKA 580
Cdd:cd14223 159 HASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEG 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 581 LLIKNPSKRLGCTGddeSASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd14223 239 LLQRDVNRRLGCMG---RGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPPRGEVNAADAFD 295
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
346-640 4.38e-50

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 178.33  E-value: 4.38e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPS--FLVALHSCFQTMDRLY 423
Cdd:cd05633   5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDcpFIVCMTYAFHTPDKLC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDAT 503
Cdd:cd05633  85 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACD--FSKKK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILY-QPYGKSVDWWAYGVLLFEMLAGQPPF---DGEDEDELFTAITEHNVSYPKSLSKEAVSLCK 579
Cdd:cd05633 163 PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSFSPELKSLLE 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426 580 ALLIKNPSKRLGCTGddeSASRDIKEHPFFRRIDWFKIETRQIQPPFKPKLKTDRSTENFD 640
Cdd:cd05633 243 GLLQRDVSKRLGCHG---RGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFD 300
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
354-609 1.72e-49

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: 173.51  E-value: 1.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTE---KRVLALPEkpsfLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd14099   9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEikiHRSLKHPN----IVKFHDCFEDEENVYILLELCS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd14099  85 NGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSL--SKEAVSLCKALLIKNPS 587
Cdd:cd14099 165 PNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQPDPT 244
                       250       260
                ....*....|....*....|..
gi 71986426 588 KRLGCTgddesasrDIKEHPFF 609
Cdd:cd14099 245 KRPSLD--------EILSHPFF 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
353-590 1.78e-49

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: 174.12  E-value: 1.78e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDV-----IIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd14084  13 TLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsRREINKPRNIETEIEILKKLSHP-CIIKIEDFFDAEDDYYIVLE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGMCKeNIFGDATT 504
Cdd:cd14084  92 LMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSK-ILGETSLM 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILY---QPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED-ELFTAITEHNVSY----PKSLSKEAVS 576
Cdd:cd14084 171 KTLCGTPTYLAPEVLRSfgtEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQmSLKEQILSGKYTFipkaWKNVSEEAKD 250
                       250
                ....*....|....
gi 71986426 577 LCKALLIKNPSKRL 590
Cdd:cd14084 251 LVKKMLVVDPSRRP 264
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
348-589 4.22e-49

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: 172.57  E-value: 4.22e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPH-IIRIYEVFENKDKIVIVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMckENIFGDAT-TKT 506
Cdd:cd14073  82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGL--SNLYSKDKlLQT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSkEAVSLCKALLIKN 585
Cdd:cd14073 160 FCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWMLTVN 238

                ....
gi 71986426 586 PSKR 589
Cdd:cd14073 239 PKRR 242
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
348-592 8.20e-49

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: 171.79  E-value: 8.20e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL-KKDVIIQDDDVEctmTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd14083   5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIdKKALKGKEDSLE---NEIAVLRKIKHPN-IVQLLDIYESKSHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM---LERDGHIKITDFGMCKenIFGDAT 503
Cdd:cd14083  81 ELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDSGV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT----EHNVSYPKSLSKEAVSLCK 579
Cdd:cd14083 159 MSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILkaeyEFDSPYWDDISDSAKDFIR 238
                       250
                ....*....|...
gi 71986426 580 ALLIKNPSKRLGC 592
Cdd:cd14083 239 HLMEKDPNKRYTC 251
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
348-607 1.57e-48

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 170.97  E-value: 1.57e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDvectMTEKRVLALPE-KPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEH----MIENEVAILRRvKHPNIVQLIEEYDTDTELYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG----HIKITDFGM---CKENIF 499
Cdd:cd14095  78 ELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLateVKEPLF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 gdattkTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED--EDELFTAITEHNVSYPK----SLSKE 573
Cdd:cd14095 158 ------TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDrdQEELFDLILAGEFEFLSpywdNISDS 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 71986426 574 AVSLCKALLIKNPSKRLgctgddeSASrDIKEHP 607
Cdd:cd14095 232 AKDLISRMLVVDPEKRY-------SAG-QVLDHP 257
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
354-609 3.25e-48

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: 170.13  E-value: 3.25e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLvALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14081   9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVL-KLYDVYENKKYLYLVLEYVSGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDaTTKTFCGTPDY 513
Cdd:cd14081  88 LFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGS-LLETSCGSPHY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 514 IAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRLgc 592
Cdd:cd14081 167 ACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEKRI-- 244
                       250
                ....*....|....*..
gi 71986426 593 tgddesASRDIKEHPFF 609
Cdd:cd14081 245 ------TIEEIKKHPWF 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
347-609 3.81e-48

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: 169.69  E-value: 3.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLK------KDVIIQdddvectmtEKRVLALPEKPsFLVALHSCFQTMD 420
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINleskekKESILN---------EIAILKKCKHP-NIVKYYGSYLKKD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGGDLmYQIQQV--GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI 498
Cdd:cd05122  71 ELWIVMEFCSGGSL-KDLLKNtnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 fGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFdgeDEDELFTAI--TEHNVSY----PKSLSK 572
Cdd:cd05122 150 -DGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY---SELPPMKALflIATNGPPglrnPKKWSK 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71986426 573 EAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFF 609
Cdd:cd05122 226 EFKDFLKKCLQKDPEKR--------PTAEQLLKHPFI 254
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
347-656 6.01e-47

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 170.24  E-value: 6.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKpSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05627   3 DFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADG-AWVVKMFYSFQDKRNLYLIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK----------- 495
Cdd:cd05627  82 EFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTglkkahrtefy 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 -------------ENIFGDATTKTF-----------CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd05627 162 rnlthnppsdfsfQNMNSKRKAETWkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSET 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 552 EDELFTAIT--EHNVSYPKS--LSKEAVSLCKALLIkNPSKRLGCTGDDEsasrdIKEHPFFRRIDWFKIETRQIQPPFk 627
Cdd:cd05627 242 PQETYRKVMnwKETLVFPPEvpISEKAKDLILRFCT-DAENRIGSNGVEE-----IKSHPFFEGVDWEHIRERPAAIPI- 314
                       330       340       350
                ....*....|....*....|....*....|...
gi 71986426 628 pKLKTDRSTENFD----HSFLKLPTKMTPPDWE 656
Cdd:cd05627 315 -EIKSIDDTSNFDdfpeSDILQPAPNTTEPDYK 346
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
348-592 8.22e-47

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 167.48  E-value: 8.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTE-KRVlalpeKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVlKRI-----KHENIVTLEDIYESTTHYYLVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd14166  80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQNGIMS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKtfCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK----SLSKEAVSLCK 579
Cdd:cd14166 160 TA--CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESpfwdDISESAKDFIR 237
                       250
                ....*....|...
gi 71986426 580 ALLIKNPSKRLGC 592
Cdd:cd14166 238 HLLEKNPSKRYTC 250
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
347-593 5.96e-46

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 164.10  E-value: 5.96e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDdVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKE-REDSVNEIRLLASVNHP-NIIRYKEAFLDGNRLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGDA 502
Cdd:cd08530  79 EYAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLKKN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDEL--------FTAItehnvsyPKSLSKEA 574
Cdd:cd08530 157 LAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELrykvcrgkFPPI-------PPVYSQDL 229
                       250
                ....*....|....*....
gi 71986426 575 VSLCKALLIKNPSKRLGCT 593
Cdd:cd08530 230 QQIIRSLLQVNPKKRPSCD 248
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
347-589 7.38e-46

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: 163.80  E-value: 7.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIK-VLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqIVKRKVAGNDKNLQLFQREINILKSLEHPG-IVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG--HIKITDFGMCKEnIFGDAT 503
Cdd:cd14098  80 MEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV-IHTGTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIIL-----YQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHnvSYPK------SLS 571
Cdd:cd14098 159 LVTFCGTMAYLAPEILMskeqnLQGgYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKG--RYTQpplvdfNIS 236
                       250
                ....*....|....*...
gi 71986426 572 KEAVSLCKALLIKNPSKR 589
Cdd:cd14098 237 EEAIDFILRLLDVDPEKR 254
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
348-592 1.01e-45

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: 163.66  E-value: 1.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqdDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVME 427
Cdd:cd14167   5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKAL---EGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM---LERDGHIKITDFGMCKENIFGDATT 504
Cdd:cd14167  82 LVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEGSGSVMS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 kTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT----EHNVSYPKSLSKEAVSLCKA 580
Cdd:cd14167 162 -TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILkaeyEFDSPYWDDISDSAKDFIQH 240
                       250
                ....*....|..
gi 71986426 581 LLIKNPSKRLGC 592
Cdd:cd14167 241 LMEKDPEKRFTC 252
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
354-609 1.51e-45

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: 162.82  E-value: 1.51e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFlVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14079  10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHI-IRLYEVIETPTDIFMVMEYVSGGE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMckENIFGDAT-TKTFCGTPD 512
Cdd:cd14079  89 LFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL--SNIMRDGEfLKTSCGSPN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEII---LYQpyGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd14079 167 YAAPEVIsgkLYA--GPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKR 244
                       250       260
                ....*....|....*....|
gi 71986426 590 LgctgddesASRDIKEHPFF 609
Cdd:cd14079 245 I--------TIPEIRQHPWF 256
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
347-608 2.39e-45

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 162.43  E-value: 2.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiQDDDVECTMT-EKRVLALPEKPSFLvALHSCFQTMDRLYFV 425
Cdd:cd14116   6 DFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQL-EKAGVEHQLRrEVEIQSHLRHPNIL-RLYGYFHDATRVYLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMckeNIFGDATTK 505
Cdd:cd14116  84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGW---SVHAPSSRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 -TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIK 584
Cdd:cd14116 161 tTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKH 240
                       250       260
                ....*....|....*....|....
gi 71986426 585 NPSKRLgctgddesASRDIKEHPF 608
Cdd:cd14116 241 NPSQRP--------MLREVLEHPW 256
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
348-589 3.79e-45

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 161.66  E-value: 3.79e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPH-IISVYEVFENSSKIVIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMckENIF-GDATTKT 506
Cdd:cd14161  83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL--SNLYnQDKFLQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSkEAVSLCKALLIKN 585
Cdd:cd14161 161 YCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLMVN 239

                ....
gi 71986426 586 PSKR 589
Cdd:cd14161 240 PERR 243
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
348-608 3.90e-45

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 161.93  E-value: 3.90e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqdDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC----RGREVCESELNVLRRVRHT-NIIQLIEVFETKERVYMVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGMCKENIFGD-AT 503
Cdd:cd14087  78 LATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKGPnCL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCK 579
Cdd:cd14087 158 MKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSgepwPSVSNLAKDFID 237
                       250       260
                ....*....|....*....|....*....
gi 71986426 580 ALLIKNPSKRLgctgddeSASRDIKeHPF 608
Cdd:cd14087 238 RLLTVNPGERL-------SATQALK-HPW 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
347-591 4.68e-45

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 161.85  E-value: 4.68e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL---------KKDVIIQDDDVECTMTEKRVLALPE--KPSFLVALHSC 415
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkKEREKRLEKEISRDIRTIREAALSSllNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 416 FQTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMck 495
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 ENIFGDATT-KTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKE 573
Cdd:cd14077 160 SNLYDPRRLlRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSE 239
                       250
                ....*....|....*...
gi 71986426 574 AVSLCKALLIKNPSKRLG 591
Cdd:cd14077 240 CKSLISRMLVVDPKKRAT 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
348-609 1.05e-44

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: 160.45  E-value: 1.05e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVlkkdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKK----MRLRKQNKELIINEILIMKECKHPN-IVDYYDSYLVGDELWVVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd06614  77 YMDGGSLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE---HNVSYPKSLSKEAVSLCKALLI 583
Cdd:cd06614 157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTkgiPPLKNPEKWSPEFKDFLNKCLV 236
                       250       260
                ....*....|....*....|....*.
gi 71986426 584 KNPSKRLGCTgddesasrDIKEHPFF 609
Cdd:cd06614 237 KDPEKRPSAE--------ELLQHPFL 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
347-608 1.08e-44

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: 160.50  E-value: 1.08e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPK-RGKSEKELRNLRQEIEILRKLNHPN-IIEMLDSFETKKEFVVVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGgDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd14002  80 EYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14002 159 IKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDP 238
                       250       260
                ....*....|....*....|..
gi 71986426 587 SKRLGCTgddesasrDIKEHPF 608
Cdd:cd14002 239 SKRLSWP--------DLLEHPF 252
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
348-589 1.06e-43

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: 157.73  E-value: 1.06e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGE--QKTTKELFAIKVLKKDvIIQDDDVEctmteKrvlALPEKPSFLVAL--------HSCFQ 417
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEytKSGLKEKVACKIIDKK-KAPKDFLE-----K---FLPRELEILRKLrhpniiqvYSIFE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 TMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG---MC 494
Cdd:cd14080  73 RGSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarLC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 KENiFGDATTKTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS---L 570
Cdd:cd14080 153 PDD-DGDVLSKTFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSvkkL 231
                       250
                ....*....|....*....
gi 71986426 571 SKEAVSLCKALLIKNPSKR 589
Cdd:cd14080 232 SPECKDLIDQLLEPDPTKR 250
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
354-590 2.57e-43

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 156.73  E-value: 2.57e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDviiqdddvecTMTEKRVLALPEKPSFLVALH--------SCFQTMDRLYFV 425
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKILDKT----------KLDQKTQRLLSREISSMEKLHhpniirlyEVVETLSKLHLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG---MCKEnifgDA 502
Cdd:cd14075  80 MEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKR----GE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKAL 581
Cdd:cd14075 156 TLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGI 235

                ....*....
gi 71986426 582 LIKNPSKRL 590
Cdd:cd14075 236 LQPVPSDRY 244
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
347-640 4.92e-43

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 159.43  E-value: 4.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKpSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05628   2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADS-LWVVKMFYSFQDKLNLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK----------- 495
Cdd:cd05628  81 EFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTglkkahrtefy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 -------------ENIFGDATTKTF-----------CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd05628 161 rnlnhslpsdftfQNMNSKRKAETWkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSET 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 552 EDELFTAIT--EHNVSYPKS--LSKEAVSLCKALLIKNpSKRLGCTGDDEsasrdIKEHPFFRRIDWFKIETRQIQPPFk 627
Cdd:cd05628 241 PQETYKKVMnwKETLIFPPEvpISEKAKDLILRFCCEW-EHRIGAPGVEE-----IKTNPFFEGVDWEHIRERPAAIPI- 313
                       330
                ....*....|...
gi 71986426 628 pKLKTDRSTENFD 640
Cdd:cd05628 314 -EIKSIDDTSNFD 325
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
354-589 8.56e-43

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: 154.62  E-value: 8.56e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKelFAIKVLKKDVIiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTD--VAIKKLKVEDD-NDELLKEFRREVSILSKLRHPN-IVQFIGACLSPPPLCIVTEYMPGGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQ-QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd13999  77 LYDLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV--SYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd13999 157 WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLrpPIPPDCPPELSKLIKRCWNEDPEKR 235
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
354-590 1.27e-42

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: 154.35  E-value: 1.27e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKdviiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPK----RDKKKEAVLREISILNQLQHPR-IIQLHEAYESPTELVLILELCSGGE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE--RDGHIKITDFGMCKEnIFGDATTKTFCGTP 511
Cdd:cd14006  76 LLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARK-LNPGEELKEIFGTP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS----YPKSLSKEAVSLCKALLIKNPS 587
Cdd:cd14006 155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseeYFSSVSQEAKDFIRKLLVKEPR 234

                ...
gi 71986426 588 KRL 590
Cdd:cd14006 235 KRP 237
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
347-625 2.05e-42

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 154.64  E-value: 2.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLvALHSCFQTMDRLYFVM 426
Cdd:cd14117   7 DFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNIL-RLYNYFHDRKRIYLIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifGDATTKT 506
Cdd:cd14117  86 EYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHA--PSLRRRT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14117 164 MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHP 243
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71986426 587 SKRLgctgddesASRDIKEHPffrridWFKIETRQIQPP 625
Cdd:cd14117 244 SERL--------PLKGVMEHP------WVKANSRRVLPP 268
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
354-608 2.69e-42

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 154.66  E-value: 2.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVecTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14169  11 LGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAM--VENEIAVLRRINHEN-IVSLEDIYESPTHLYLAMELVTGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE---RDGHIKITDFGMCKenIFGDATTKTFCGT 510
Cdd:cd14169  88 LFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQGMLSTACGT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT----EHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14169 166 PGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILkaeyEFDSPYWDDISESAKDFIRHLLERDP 245
                       250       260
                ....*....|....*....|..
gi 71986426 587 SKRLGCtgddESASRdikeHPF 608
Cdd:cd14169 246 EKRFTC----EQALQ----HPW 259
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
348-589 6.96e-41

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: 149.98  E-value: 6.96e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDK-TQLNPSSLQKLFREVRIMKILNHPN-IVKLFEVIETEKTLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDaTTKTF 507
Cdd:cd14072  80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGN-KLDTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14072 159 CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNP 238

                ...
gi 71986426 587 SKR 589
Cdd:cd14072 239 SKR 241
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
348-608 1.42e-40

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 150.58  E-value: 1.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL-KKDVIIQDDDVECTMTEKRVLalpeKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd14168  12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIpKKALKGKESSIENEIAVLRKI----KHENIVALEDIYESPNHLYLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd14168  88 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGDVM 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TkTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT----EHNVSYPKSLSKEAVSLCK 579
Cdd:cd14168 168 S-TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILkadyEFDSPYWDDISDSAKDFIR 246
                       250       260
                ....*....|....*....|....*....
gi 71986426 580 ALLIKNPSKRLGCtgddESASRdikeHPF 608
Cdd:cd14168 247 NLMEKDPNKRYTC----EQALR----HPW 267
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
354-608 1.45e-40

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: 149.37  E-value: 1.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKdviiqdddveCTMTE--KRVLALPE-KPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd14010   8 IGRGKHSVVYKGRRKGTIEFVAIKCVDK----------SKRPEvlNEVRLTHElKHPNVLKFYEWYETSNHLWLVVEYCT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDATTKTFC-- 508
Cdd:cd14010  78 GGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARR--EGEILKELFGqf 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 ----------------GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK---- 568
Cdd:cd14010 156 sdegnvnkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPpkvs 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71986426 569 -SLSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPF 608
Cdd:cd14010 236 sKPSPDFKSLLKGLLEKDPAKRLSWD--------ELVKHPF 268
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
347-608 1.72e-40

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 148.86  E-value: 1.72e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLvALHSCFQTMDRLYFVM 426
Cdd:cd14186   2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSIL-ELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd14186  81 EMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKN 585
Cdd:cd14186 161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                       250       260
                ....*....|....*....|...
gi 71986426 586 PSKRLGCTGddesasrdIKEHPF 608
Cdd:cd14186 241 PADRLSLSS--------VLDHPF 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
346-613 6.16e-40

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: 147.35  E-value: 6.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVlkkdvIIQDDDVECT---MTEKRVLALPEKPsFLVALHSCFQTMDRL 422
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKK-----IHVDGDEEFRkqlLRELKTLRSCESP-YVVKCYGAFYKEGEI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCK--ENif 499
Cdd:cd06623  75 SIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKvlEN-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEA----- 574
Cdd:cd06623 153 TLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPSLPAEEfspef 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71986426 575 ---VSLCkalLIKNPSKRLGCTgddesasrDIKEHPFFRRID 613
Cdd:cd06623 233 rdfISAC---LQKDPKKRPSAA--------ELLQHPFIKKAD 263
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
353-608 1.29e-39

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 146.63  E-value: 1.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVecTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14185   7 TIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDM--IESEILIIKSLSHPN-IVKLFEVYETEKEIYLILEYVRGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH----IKITDFGMCK---ENIFgdattk 505
Cdd:cd14185  84 DLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDksttLKLADFGLAKyvtGPIF------ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGE--DEDELFTAIT----EHNVSYPKSLSKEAVSLCK 579
Cdd:cd14185 158 TVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQlghyEFLPPYWDNISEAAKDLIS 237
                       250       260
                ....*....|....*....|....*....
gi 71986426 580 ALLIKNPSKRLgctgddesASRDIKEHPF 608
Cdd:cd14185 238 RLLVVDPEKRY--------TAKQVLQHPW 258
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
354-608 2.44e-39

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: 145.62  E-value: 2.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVlkkdVIIQDDD------VECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKE----VSLVDDDkksresVKQLEQEIALLSKLRHPN-IVQYYGTEREEDNLYIFLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTKTF 507
Cdd:cd06632  83 YVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAKSF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQ--PYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITEHNV-SYPKSLSKEA---VSLCka 580
Cdd:cd06632 162 KGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWsQYEGVAAIFKIGNSGELpPIPDHLSPDAkdfIRLC-- 239
                       250       260
                ....*....|....*....|....*...
gi 71986426 581 lLIKNPSKRLGCTgddesasrDIKEHPF 608
Cdd:cd06632 240 -LQRDPEDRPTAS--------QLLEHPF 258
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
351-590 3.37e-39

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 145.70  E-value: 3.37e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLG------EQKTTKELfAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYF 424
Cdd:cd14076   6 GRTLGEGEFGKVKLGwplpkaNHRSGVQV-AIKLIRRDTQQENCQTSKIMREINILKGLTHPN-IVRLLDVLKTKKYIGI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE-NIFGDAT 503
Cdd:cd14076  84 VLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPE-IILYQPY-GKSVDWWAYGVLLFEMLAGQPPFD-------GEDEDELFTAITEHNVSYPKSLSKEA 574
Cdd:cd14076 164 MSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFDddphnpnGDNVPRLYRYICNTPLIFPEYVTPKA 243
                       250
                ....*....|....*.
gi 71986426 575 VSLCKALLIKNPSKRL 590
Cdd:cd14076 244 RDLLRRILVPNPRKRI 259
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
354-590 5.72e-39

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 144.45  E-value: 5.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqDDDVECTMTEKRVLalpekpSFLVALHSC-----FQTMDRLYFVMEF 428
Cdd:cd14078  11 IGSGGFAKVKLATHILTGEKVAIKIMDKKAL--GDDLPRVKTEIEAL------KNLSHQHICrlyhvIETDNKIFMVLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG-DATTKTF 507
Cdd:cd14078  83 CPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGmDHHLETC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14078 163 CGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDP 242

                ....
gi 71986426 587 SKRL 590
Cdd:cd14078 243 KKRI 246
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
352-590 7.88e-39

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: 144.42  E-value: 7.88e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEcTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd14106  14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNE-ILHEIAVLELCKDCPRVVNLHEVYETRSELILILELAAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD---GHIKITDFGMCKEnIFGDATTKTFC 508
Cdd:cd14106  93 GELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRV-IGEGEEIREIL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCKALLIK 584
Cdd:cd14106 172 GTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPeelfKDVSPLAIDFIKRLLVK 251

                ....*.
gi 71986426 585 NPSKRL 590
Cdd:cd14106 252 DPEKRL 257
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
37-94 2.16e-38

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410383  Cd Length: 58  Bit Score: 136.00  E-value: 2.16e-38
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426  37 KSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADKG 94
Cdd:cd20833   1 KDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCSFVVHKRCHEFVTFSCPGADKG 58
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
354-613 2.42e-38

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: 144.10  E-value: 2.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVL--KKdviIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd14086   9 LGKGAFSVVRRCVQKSTGQEFAAKIIntKK---LSARDHQKLEREARICRLLKHPN-IVRLHDSISEEGFHYLVFDLVTG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENIFGDATTKTFC 508
Cdd:cd14086  85 GELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGFA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK----SLSKEAVSLCKALLIK 584
Cdd:cd14086 165 GTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLINQMLTV 244
                       250       260
                ....*....|....*....|....*....
gi 71986426 585 NPSKRLgctgddeSASRDIKeHPFFRRID 613
Cdd:cd14086 245 NPAKRI-------TAAEALK-HPWICQRD 265
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
104-157 1.17e-37

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 133.62  E-value: 1.17e-37
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCGTDN 157
Cdd:cd20836   1 HKFKVHTYSSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKRCVKNVPSLCGTDH 54
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
346-609 1.87e-37

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: 140.54  E-value: 1.87e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKV-------------LKKDVIIQDddvecTMTEKRVLAL---PEKPSFl 409
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFvdmkrapgdcpenIKKEVCIQK-----MLSHKNVVRFyghRREGEF- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 410 valhscfqtmdrLYFVMEFVNGGDLMYQIQ-QVGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI 488
Cdd:cd14069  75 ------------QYLFLEYASGGELFDKIEpDVG-MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 489 TDFGMC-------KENIFGDAttktfCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFD-GEDEDELFTA- 558
Cdd:cd14069 142 SDFGLAtvfrykgKERLLNKM-----CGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDqPSDSCQEYSDw 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71986426 559 ITEHNVSY-P-KSLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14069 217 KENKKTYLtPwKKIDTAALSLLRKILTENPNKRI--------TIEDIKKHPWY 261
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
348-590 2.41e-37

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 140.38  E-value: 2.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPE-KPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINRE---KAGSSAVKLLEREVDILKHvNHAHIIHLEEVFETPKRMYLVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG-------HIKITDFGMC-KENI 498
Cdd:cd14097  80 ELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvQKYG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 FGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEA 574
Cdd:cd14097 160 LGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAA 239
                       250
                ....*....|....*.
gi 71986426 575 VSLCKALLIKNPSKRL 590
Cdd:cd14097 240 KNVLQQLLKVDPAHRM 255
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
354-609 2.47e-37

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: 140.46  E-value: 2.47e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEcTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14197  17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRME-IIHEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQI--QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD---GHIKITDFGMCKEnIFGDATTKTFC 508
Cdd:cd14197  96 IFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRI-LKNSEELREIM 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS----LSKEAVSLCKALLIK 584
Cdd:cd14197 175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEefehLSESAIDFIKTLLIK 254
                       250       260
                ....*....|....*....|....*
gi 71986426 585 NPSKRlgctgddeSASRDIKEHPFF 609
Cdd:cd14197 255 KPENR--------ATAEDCLKHPWL 271
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
354-589 3.86e-37

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: 139.68  E-value: 3.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVII---QDDDVECTMTEKRVLALPEkpsfLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd14187  15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLkphQKEKMSMEIAIHRSLAHQH----VVGFHGFFEDNDFVYVVLELCR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd14187  91 RRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGT 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd14187 171 PNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 249
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
346-606 4.64e-37

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 139.92  E-value: 4.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLA--LPEKPSFLVALHSCFQTMDRLY 423
Cdd:cd06917   1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT--DDDDVSDIQKEVALLSqlKLGQPKNIIKYYGSYLKGPSLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd06917  79 IIMDYCEGGSIR-TLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILY-QPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV------SYPKSLsKEAVS 576
Cdd:cd06917 158 RSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPprlegnGYSPLL-KEFVA 236
                       250       260       270
                ....*....|....*....|....*....|
gi 71986426 577 LCkalLIKNPSKRLgcTGDDESASRDIKEH 606
Cdd:cd06917 237 AC---LDEEPKDRL--SADELLKSKWIKQH 261
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
346-611 6.97e-37

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 139.30  E-value: 6.97e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLkkDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVI--DLEEAEDEIEDIQQEIQFLSQCDSP-YITKYYGSFLKGSKLWII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGG---DLMyqiqQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDA 502
Cdd:cd06609  78 MEYCGGGsvlDLL----KPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNvsyPKSLS--------KEA 574
Cdd:cd06609 154 KRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNN---PPSLEgnkfskpfKDF 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71986426 575 VSLCkalLIKNPSKRlgctgddeSASRDIKEHPFFRR 611
Cdd:cd06609 231 VELC---LNKDPKER--------PSAKELLKHKFIKK 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
354-589 7.05e-37

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: 138.51  E-value: 7.05e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd06627   8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSV-MGEIDLLKKLNHPN-IVKYIGSVKTKDSLYIILEYVENGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDATTKTF--CGTP 511
Cdd:cd06627  86 LASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATK--LNEVEKDENsvVGTP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTAITEHNVSYPKSLSKEavslCKALLI----KNP 586
Cdd:cd06627 164 YWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyYDLQPMAALFRIVQDDHPPLPENISPE----LRDFLLqcfqKDP 239

                ...
gi 71986426 587 SKR 589
Cdd:cd06627 240 TLR 242
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
347-589 1.33e-36

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 137.80  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIR--LPKSSSAVEDSRKEAVLLAKMKHPN-IVAFKESFEADGHLYIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQI-QQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATT 504
Cdd:cd08219  78 EYCDGGDLMQKIkLQRGKlFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS-YPKSLSKEAVSLCKALLI 583
Cdd:cd08219 158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFK 237

                ....*.
gi 71986426 584 KNPSKR 589
Cdd:cd08219 238 RNPRSR 243
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
347-609 2.72e-36

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: 137.05  E-value: 2.72e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLE---PGDDFEIIQQEISMLKECRHPN-IVAYFGSYLRRDKLWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd06613  77 EYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQ---PYGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTaITEHNVSYPKSLSKEAVSL----- 577
Cdd:cd06613 157 FIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPmFDLHPMRALFL-IPKSNFDPPKLKDKEKWSPdfhdf 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 71986426 578 CKALLIKNPSKRlgctgddESASRDIKeHPFF 609
Cdd:cd06613 236 IKKCLTKNPKKR-------PTATKLLQ-HPFV 259
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
354-589 6.62e-36

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 136.59  E-value: 6.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEcTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14198  16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAE-ILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAGGE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQI--QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD---GHIKITDFGMCKEniFGDATT-KTF 507
Cdd:cd14198  95 IFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK--IGHACElREI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK----SLSKEAVSLCKALLI 583
Cdd:cd14198 173 MGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsSVSQLATDFIQKLLV 252

                ....*.
gi 71986426 584 KNPSKR 589
Cdd:cd14198 253 KNPEKR 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
346-610 8.21e-36

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 135.65  E-value: 8.21e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKvlKKDVIIQDDDvECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:cd06648   7 SDLDNFVKIGEGSTGIVCIATDKSTGRQVAVK--KMDLRKQQRR-ELLFNEVVIMRDYQHPN-IVEMYSSYLVGDELWVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAeIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd06648  83 MEFLEGGALTDIVTHTRMNEEQIATVCRA-VLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH---NVSYPKSLSKEAVSLCKALL 582
Cdd:cd06648 162 SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNeppKLKNLHKVSPRLRSFLDRML 241
                       250       260
                ....*....|....*....|....*...
gi 71986426 583 IKNPSKRlgctgddeSASRDIKEHPFFR 610
Cdd:cd06648 242 VRDPAQR--------ATAAELLNHPFLA 261
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
353-609 1.03e-35

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 135.21  E-value: 1.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14071   7 TIGKGNFAVVKLARHRITKTEVAIKIIDKSQL-DEENLKKIYREVQIMKMLNHPH-IIKLYQVMETKDMLYLVTEYASNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMckENIF-GDATTKTFCGTP 511
Cdd:cd14071  85 EIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF--SNFFkPGELLKTWCGSP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd14071 163 PYAAPEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSKRL 242
                       250
                ....*....|....*....
gi 71986426 591 GCtgddesasRDIKEHPFF 609
Cdd:cd14071 243 TI--------EQIKKHKWM 253
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
353-584 1.35e-35

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


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 135.12  E-value: 1.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14162   7 TLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPN-LICFYEAIETTSRVYIIMELAENG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT----TKTFC 508
Cdd:cd14162  86 DLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGkpklSETYC 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEI---ILYQPYgkSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAItEHNVSYPKS--LSKEavslCKALLI 583
Cdd:cd14162 166 GSYAYASPEIlrgIPYDPF--LSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPKNptVSEE----CKDLIL 238

                .
gi 71986426 584 K 584
Cdd:cd14162 239 R 239
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
354-608 2.09e-35

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: 134.82  E-value: 2.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIK--VLKKDVIIQDDDVECTM-----TEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKqvELPKTSSDRADSRQKTVvdalkSEIDTLKDLDHPN-IVQYLGFEETEDYFSIFL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFGDATT 504
Cdd:cd06629  88 EYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKksDDIYGNNGA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEII--LYQPYGKSVDWWAYGVLLFEMLAGQPPFdgeDEDELFTAITEhnVSYPKS---------LSKE 573
Cdd:cd06629 168 TSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFK--LGNKRSappvpedvnLSPE 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71986426 574 AVSLCKALLIKNPSKRlgctgddeSASRDIKEHPF 608
Cdd:cd06629 243 ALDFLNACFAIDPRDR--------PTAAELLSHPF 269
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
354-609 2.34e-35

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 134.52  E-value: 2.34e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMD-RLYFVMEFVNGG 432
Cdd:cd14165   9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKS-IIKTYEIFETSDgKVYIVMELGVQG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGD----ATTKTFC 508
Cdd:cd14165  88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEngriVLSKTFC 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSV-DWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS--LSKEAVSLCKALLIKN 585
Cdd:cd14165 168 GSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSknLTSECKDLIYRLLQPD 247
                       250       260
                ....*....|....*....|....
gi 71986426 586 PSKRLGCtgdDEsasrdIKEHPFF 609
Cdd:cd14165 248 VSQRLCI---DE-----VLSHPWL 263
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
347-589 2.73e-35

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: 134.59  E-value: 2.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiqdddvecTMTEKR-------VLALPE-KPSFLVALHSCFQt 418
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYG----------KMSEKEkqqlvseVNILRElKHPNIVRYYDRIV- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 mDR----LYFVMEFVNGGDLMYQIQQVGKFKEPVA------VFYaaEIAVGLFFLHSKG-----IIYRDLKLDNVMLERD 483
Cdd:cd08217  70 -DRanttLYIVMEYCEGGDLAQLIKKCKKENQYIPeefiwkIFT--QLLLALYECHNRSvgggkILHRDLKPANIFLDSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 484 GHIKITDFGMCKenIFGDAT--TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd08217 147 NNVKLGDFGLAR--VLSHDSsfAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKE 224
                       250       260
                ....*....|....*....|....*....
gi 71986426 562 HNVS-YPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd08217 225 GKFPrIPSRYSSELNEVIKSMLNVDPDKR 253
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
354-590 6.95e-35

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: 133.38  E-value: 6.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVI------IQDDDVEctmTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14105  13 LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIE---REVSILRQVLHPN-IITLHDVFENKTDVVLILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERD---GHIKITDFGMCKENIFGdAT 503
Cdd:cd14105  89 LVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLlDKNvpiPRIKLIDFGLAHKIEDG-NE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS----YPKSLSKEAVSLCK 579
Cdd:cd14105 168 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDfddeYFSNTSELAKDFIR 247
                       250
                ....*....|.
gi 71986426 580 ALLIKNPSKRL 590
Cdd:cd14105 248 QLLVKDPRKRM 258
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
353-609 8.49e-35

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 132.74  E-value: 8.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVL---------KKDVIIQDDDVECTMTEKRVlalpekpsflVALHSCFQTMDRLY 423
Cdd:cd14189   8 LLGKGGFARCYEMTDLATNKTYAVKVIphsrvakphQREKIVNEIELHRDLHHKHV----------VKFSHHFEDAENIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd14189  78 IFLELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLI 583
Cdd:cd14189 158 KKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILK 237
                       250       260
                ....*....|....*....|....*.
gi 71986426 584 KNPSKRLgcTGDdesasrDIKEHPFF 609
Cdd:cd14189 238 RNPGDRL--TLD------QILEHEFF 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
354-608 1.18e-34

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 132.54  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqdDDVECT--MTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd14074  11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKL---DDVSKAhlFQEVRCMKLVQHPN-VVRLYEVIDTQTKLYLILELGDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERDGHIKITDFGMCKENIFGDATTkTFCG 509
Cdd:cd14074  87 GDMYdYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKLE-TSCG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPSK 588
Cdd:cd14074 166 SLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDPKK 245
                       250       260
                ....*....|....*....|.
gi 71986426 589 RlgctgddesAS-RDIKEHPF 608
Cdd:cd14074 246 R---------ASlEEIENHPW 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
348-590 1.18e-34

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 132.42  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIqDDDVECTMTEKRVLALPEkpsfLVALHSCFQTMDRLYFVME 427
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKI-DENVQREIINHRSLRHPN----IVRFKEVILTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLerDG----HIKITDFGMCKENIFgDAT 503
Cdd:cd14665  77 YAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL--DGspapRLKICDFGYSKSSVL-HSQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH--NVSY--PK--SLSKEAVS 576
Cdd:cd14665 154 PKSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRilSVQYsiPDyvHISPECRH 233
                       250
                ....*....|....
gi 71986426 577 LCKALLIKNPSKRL 590
Cdd:cd14665 234 LISRIFVADPATRI 247
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
347-609 1.37e-34

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: 132.00  E-value: 1.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKrvlalpEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd06612   4 VFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQ------CDSPYIVKYYGSYFKNTDLWIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGG---DLMYQIQQVgkFKEpvavfyaAEIAV-------GLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd06612  78 EYCGAGsvsDIMKITNKT--LTE-------EEIAAilyqtlkGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTAITE--HNVSYPKSLSKE 573
Cdd:cd06612 149 LTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPySDIHPMRAIFMIPNKppPTLSDPEKWSPE 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 574 AVSLCKALLIKNPSKRlgctgddESASrDIKEHPFF 609
Cdd:cd06612 229 FNDFVKKCLVKDPEER-------PSAI-QLLQHPFI 256
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
353-609 1.69e-34

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: 132.48  E-value: 1.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVL-----KKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVME 427
Cdd:cd14093  10 ILGRGVSSTVRRCIEKETGQEFAVKIIditgeKSSENEAEELREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDaTTKTF 507
Cdd:cd14093  90 LCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGE-KLREL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQ------PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK----SLSKEAVSL 577
Cdd:cd14093 169 CGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSpewdDISDTAKDL 248
                       250       260       270
                ....*....|....*....|....*....|..
gi 71986426 578 CKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14093 249 ISKLLVVDPKKRL--------TAEEALEHPFF 272
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
354-589 2.46e-34

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 131.86  E-value: 2.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMT-EKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14070  10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRrEGRIQQMIRHPN-ITQLLDILETENSYYLVMELCPGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGM--CKENIFGDATTKTFCGT 510
Cdd:cd14070  89 NLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSDPFSTQCGS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGE--DEDELFTAITEHNVS-YPKSLSKEAVSLCKALLIKNPS 587
Cdd:cd14070 169 PAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMNpLPTDLSPGAISFLRSLLEPDPL 248

                ..
gi 71986426 588 KR 589
Cdd:cd14070 249 KR 250
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
350-561 2.59e-34

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: 131.52  E-value: 2.59e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    350 FLTVLGKGSFGKVLLGE----QKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDA--SEQQIEEFLREARIMRKLDHPN-IVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    426 MEFVNGGDLMYQIQQVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDAT 503
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPKELSLSdlLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD-LYDDDY 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426    504 TKTFCGT-P-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE 561
Cdd:smart00221 159 YKVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKK 219
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
347-589 3.00e-34

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 131.38  E-value: 3.00e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEA-IDEARVLSKLNSP-YVIKYYDSFVDKGKLNIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQ-QVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGDAT- 503
Cdd:cd08529  79 EYAENGDLHSLIKsQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK--ILSDTTn 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 -TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS-YPKSLSKEAVSLCKAL 581
Cdd:cd08529 157 fAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSC 236

                ....*...
gi 71986426 582 LIKNPSKR 589
Cdd:cd08529 237 LTKDYRQR 244
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
354-590 3.95e-34

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: 130.95  E-value: 3.95e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLG-EQKTTKELFAIKVLKKDVIIQDDdvecTMTEKRVLALPE-KPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd14120   1 IGHGAFAVVFKGrHRKKPDLPVAIKCITKKNLSKSQ----NLLGKEIKILKElSHENVVALLDCQETSSSVYLVMEYCNG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG---------HIKITDFGMCKeNIFGDA 502
Cdd:cd14120  77 GDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFAR-FLQDGM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELfTAITEHNV----SYPKSLSKEAVSLC 578
Cdd:cd14120 156 MAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQEL-KAFYEKNAnlrpNIPSGTSPALKDLL 234
                       250
                ....*....|..
gi 71986426 579 KALLIKNPSKRL 590
Cdd:cd14120 235 LGLLKRNPKDRI 246
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
354-608 5.24e-34

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 130.66  E-value: 5.24e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIqDDDVECTMTEKRVLALPEkpsfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14662   8 IGSGNFGVARLMRNKETKELVAVKYIERGLKI-DENVQREIINHRSLRHPN----IIRFKEVVLTPTHLAIVMEYAAGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLerDG----HIKITDFGMCKENIFgDATTKTFCG 509
Cdd:cd14662  83 LFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL--DGspapRLKICDFGYSKSSVL-HSQPKSTVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELF----TAITEHNVSYPK--SLSKEAVSLCKALL 582
Cdd:cd14662 160 TPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFrktiQRIMSVQYKIPDyvRVSQDCRHLLSRIF 239
                       250       260
                ....*....|....*....|....*.
gi 71986426 583 IKNPSKRLgctgddesASRDIKEHPF 608
Cdd:cd14662 240 VANPAKRI--------TIPEIKNHPW 257
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
354-650 6.03e-34

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: 132.04  E-value: 6.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqdddveCTMTEKRVLALPEKPSFLVALHSCFQtmDRL--YFVMEFVNG 431
Cdd:cd14092  14 LGDGSFSVCRKCVHKKTGQEFAVKIVSRRL--------DTSREVQLLRLCQGHPNIVKLHEVFQ--DELhtYLVMELLRG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG---HIKITDFGMCK---ENifgdATTK 505
Cdd:cd14092  84 GELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFARlkpEN----QPLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIIL----YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED----ELFTAITEHNVSYP----KSLSKE 573
Cdd:cd14092 160 TPCFTLPYAAPEVLKqalsTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFDgeewKNVSSE 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 574 AVSLCKALLIKNPSKRLGCTgddesasrDIKEHPffrridWFKIETRQIQPPfkpklktDRSTENFDHSFLKLPTKM 650
Cdd:cd14092 240 AKSLIQGLLTVDPSKRLTMS--------ELRNHP------WLQGSSSPSSTP-------LMTPGVLSSSAAAVSTAL 295
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
353-609 6.15e-34

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 130.52  E-value: 6.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVII---QDDDVECTMTEKRVLalpeKPSFLVALHSCFQTMDRLYFVMEFV 429
Cdd:cd14188   8 VLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSkphQREKIDKEIELHRIL----HHKHVVQFYHYFEDKENIYILLEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd14188  84 SRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNPskr 589
Cdd:cd14188 164 TPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNP--- 240
                       250       260
                ....*....|....*....|
gi 71986426 590 lgctgDDESASRDIKEHPFF 609
Cdd:cd14188 241 -----EDRPSLDEIIRHDFF 255
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
354-609 1.08e-33

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: 129.68  E-value: 1.08e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQ----DDDVECTMTEKRVLALPEkpsfLVALHSCFQTMD--RLYFVME 427
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRipngEANVKREIQILRRLNHRN----VIKLVDVLYNEEkqKLYMVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGG-DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE-NIF-GDATT 504
Cdd:cd14119  77 YCVGGlQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAlDLFaEDDTC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPY--GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALL 582
Cdd:cd14119 157 TTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGML 236
                       250       260
                ....*....|....*....|....*..
gi 71986426 583 IKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14119 237 EKDPEKRF--------TIEQIRQHPWF 255
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
347-609 1.21e-33

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: 129.43  E-value: 1.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDddvecTMTEKRVLA-LPEKPSFL-----------VALHS 414
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVD-----TWVRDRKLGtVPLEIHILdtlnkrshpniVKLLD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 415 CFQTMDRLYFVME-FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG- 492
Cdd:cd14004  76 FFEDDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGs 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 493 --MCKENIFgdattKTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEdelftaITEHNVSYPKS 569
Cdd:cd14004 156 aaYIKSGPF-----DTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYA 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71986426 570 LSKEAVSLCKALLIKNPSKRlgCTGDdesasrDIKEHPFF 609
Cdd:cd14004 225 VSEDLIDLISRMLNRDVGDR--PTIE------ELLTDPWL 256
C2 pfam00168
C2 domain;
174-280 2.40e-33

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 123.20  E-value: 2.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIpedsGCKSKQKTKTLRATLNPQWNETFTYKlLPGDKDRRLSIEVWDWDRT 253
Cdd:pfam00168   2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLL----DGKQKKKTKVVKNTLNPVWNETFTFS-VPDPENAVLEIEVYDYDRF 76
                          90       100
                  ....*....|....*....|....*...
gi 71986426   254 SRNDFMGSLSFGISEL-MKEAASGWYKL 280
Cdd:pfam00168  77 GRDDFIGEVRIPLSELdSGEGLDGWYPL 104
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
354-613 2.55e-33

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 129.48  E-value: 2.55e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVlkkdVIIQD-DDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKI----IQIESeEELEDFMVEIDILSECKHPN-IVGLYEAYFYENKLWILIEFCDGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 ---DLMYQIQQVgkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd06611  88 aldSIMLELERG--LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILY-----QPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHN---VSYPKSLSKEAVSLCKAL 581
Cdd:cd06611 166 TPYWMAPEVVACetfkdNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSSFNDFLKSC 245
                       250       260       270
                ....*....|....*....|....*....|..
gi 71986426 582 LIKNPSKRLGCtgddesasRDIKEHPFFRRID 613
Cdd:cd06611 246 LVKDPDDRPTA--------AELLKHPFVSDQS 269
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
348-589 3.22e-33

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: 128.54  E-value: 3.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLK-KDVIIQDDdvECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDlTKMPVKEK--EASKKEVILLAKMKHPN-IVTFFASFQENGRLFIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQ-QVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI-KITDFGMCKenIFGDAT 503
Cdd:cd08225  79 EYCDGGDLMKRINrQRGvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIAR--QLNDSM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 --TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSyPKS--LSKEAVSLCK 579
Cdd:cd08225 157 elAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFA-PISpnFSRDLRSLIS 235
                       250
                ....*....|
gi 71986426 580 ALLIKNPSKR 589
Cdd:cd08225 236 QLFKVSPRDR 245
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
348-609 3.54e-33

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: 128.81  E-value: 3.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDddvECT-MTE-KRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWE---ECMnLREvKSLRKLNEHP-NIVKLKEVFRENDELYFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGdlMYQI---QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDA 502
Cdd:cd07830  77 FEYMEGN--LYQLmkdRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLARE-IRSRP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELFTaITE------------------- 561
Cdd:cd07830 154 PYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEiDQLYK-ICSvlgtptkqdwpegyklask 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 562 HNVSYPK-----------SLSKEAVSLCKALLIKNPSKRLgctgddeSASrDIKEHPFF 609
Cdd:cd07830 233 LGFRFPQfaptslhqlipNASPEAIDLIKDMLRWDPKKRP-------TAS-QALQHPYF 283
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
353-589 4.51e-33

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: 127.86  E-value: 4.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVlkkdVIIQDDDVEctmTEKRVLALPEKPSFLVALH--------SCFQTMDRLYF 424
Cdd:cd06625   7 LLGQGAFGQVYLCYDADTGRELAVKQ----VEIDPINTE---ASKEVKALECEIQLLKNLQherivqyyGCLQDEKSLSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFGDA 502
Cdd:cd06625  80 FMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSST 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTaITEHNVSY--PKSLSKEAVSLCK 579
Cdd:cd06625 160 GMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPwAEFEPMAAIFK-IATQPTNPqlPPHVSEDARDFLS 238
                       250
                ....*....|
gi 71986426 580 ALLIKNPSKR 589
Cdd:cd06625 239 LIFVRNKKQR 248
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
350-561 6.24e-33

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 127.65  E-value: 6.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    350 FLTVLGKGSFGKVLLGE----QKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDA--SEQQIEEFLREARIMRKLDHPN-VVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    426 MEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATT 504
Cdd:smart00219  80 MEYMEGGDLLsYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD-LYDDDYY 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    505 KTFCGT-P-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE 561
Cdd:smart00219 159 RKRGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKN 218
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
354-593 8.54e-33

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: 126.96  E-value: 8.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEctmTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVR---NEIEIMNQLRHPR-LLQLYDAFETPREMVLVMEYVAGGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LM-------YQIQqvgkfkEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LERDGH-IKITDFGM-CKENifGDAT 503
Cdd:cd14103  77 LFervvdddFELT------ERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLaRKYD--PDKK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCK 579
Cdd:cd14103 149 LKVLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDdeafDDISDEAKDFIS 228
                       250
                ....*....|....
gi 71986426 580 ALLIKNPSKRLGCT 593
Cdd:cd14103 229 KLLVKDPRKRMSAA 242
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
30-90 1.29e-32

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 119.88  E-value: 1.29e-32
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986426  30 QKNVHEIKSHKFIARFFKQPTFCSHCKDFLWGI-TKQGFQCQVCTLVVHKRCHEFVNFACPG 90
Cdd:cd20835   1 RRRVHQVNGHKFMATYLRQPTYCSHCKDFIWGViGKQGYQCQVCTCVVHKRCHQLVVTKCPG 62
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
353-609 1.80e-32

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: 125.81  E-value: 1.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiqddDVECTMTEK-----RVLALPEKPSFLVALHSCF--QTMDRLYFV 425
Cdd:cd05118   6 KIGEGAFGTVWLARDKVTGEKVAIKKIKND------FRHPKAALReikllKHLNDVEGHPNIVKLLDVFehRGGNHLCLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVnGGDL--MYQIQQVGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERDGHIKITDFGMCKenIFGDA 502
Cdd:cd05118  80 FELM-GMNLyeLIKDYPRG-LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLADFGLAR--SFTSP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEhnvsypKSLSKEAVSLCKAL 581
Cdd:cd05118 156 PYTPYVATRWYRAPEVLLgAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR------LLGTPEALDLLSKM 229
                       250       260
                ....*....|....*....|....*...
gi 71986426 582 LIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd05118 230 LKYDPAKRI--------TASQALAHPYF 249
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
354-590 2.01e-32

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: 126.29  E-value: 2.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVI------IQDDDVEctmTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14194  13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkssrrgVSREDIE---REVSILKEIQHPN-VITLHEVYENKTDVILILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERDG---HIKITDFGMCKENIFGDAT 503
Cdd:cd14194  89 LVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLlDRNVpkpRIKIIDFGLAHKIDFGNEF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFcGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT----EHNVSYPKSLSKEAVSLCK 579
Cdd:cd14194 169 KNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSavnyEFEDEYFSNTSALAKDFIR 247
                       250
                ....*....|.
gi 71986426 580 ALLIKNPSKRL 590
Cdd:cd14194 248 RLLVKDPKKRM 258
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
354-590 2.16e-32

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 127.25  E-value: 2.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqddDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14085  11 LGRGATSVVYRCRQKGTQKPYAVKKLKKTV-----DKKIVRTEIGVLLRLSHPN-IIKLKEIFETPTEISLVLELVTGGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER---DGHIKITDFGMCKEnIFGDATTKTFCGT 510
Cdd:cd14085  85 LFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKI-VDQQVTMKTVCGT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDE-LFTAI--TEHNVSYP--KSLSKEAVSLCKALLIKN 585
Cdd:cd14085 164 PGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKRIlnCDYDFVSPwwDDVSLNAKDLVKKLIVLD 243

                ....*
gi 71986426 586 PSKRL 590
Cdd:cd14085 244 PKKRL 248
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
353-608 2.56e-32

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 126.76  E-value: 2.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqdddvecTMTEKRVLALPEkpsflvALHSC------------FQTMD 420
Cdd:cd14090   9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHP---------GHSRSRVFREVE------TLHQCqghpnilqlieyFEDDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI---KITDFGM---C 494
Cdd:cd14090  74 RFYLVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLgsgI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 KENifGDATT-------KTFCGTPDYIAPEII---LYQP--YGKSVDWWAYGVLLFEMLAGQPPFDG---ED-------- 551
Cdd:cd14090 154 KLS--STSMTpvttpelLTPVGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPFYGrcgEDcgwdrgea 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 552 ----EDELFTAITEHNVSYP----KSLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPF 608
Cdd:cd14090 232 cqdcQELLFHSIQEGEYEFPekewSHISAEAKDLISHLLVRDASQRY--------TAEQVLQHPW 288
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
353-594 2.73e-32

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 127.08  E-value: 2.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQdddvecTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14179  14 PLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEAN------TQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML--ERDG-HIKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd14179  88 ELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdESDNsEIKIIDFGFARLKPPDNQPLKTPCF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-------DELFTAITEHNVSYP----KSLSKEAVSLC 578
Cdd:cd14179 168 TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKsltctsaEEIMKKIKQGDFSFEgeawKNVSQEAKDLI 247
                       250
                ....*....|....*.
gi 71986426 579 KALLIKNPSKRLGCTG 594
Cdd:cd14179 248 QGLLTVDPNKRIKMSG 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
348-589 3.68e-32

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 126.40  E-value: 3.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLG-EQKTTKELFAIKVLKK----DVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRL 422
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVRKadlsSDNLKGSSRANILKEVQIMKRLSHPN-IVKLLDFQESDEYY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER-------------------- 482
Cdd:cd14096  82 YIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkadddetkv 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 483 D-------------GHIKITDFGMCKenIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDG 549
Cdd:cd14096 162 DegefipgvggggiGIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYD 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71986426 550 EDEDELFTAITEHNVSYPK----SLSKEAVSLCKALLIKNPSKR 589
Cdd:cd14096 240 ESIETLTEKISRGDYTFLSpwwdEISKSAKDLISHLLTVDPAKR 283
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
354-612 5.17e-32

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 125.91  E-value: 5.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEILATCNHP-YIVKLLGAFYWDGKLWIMIEFCPGGA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPD 512
Cdd:cd06644  96 VDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPY 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQ-----PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHN---VSYPKSLSKEAVSLCKALLIK 584
Cdd:cd06644 176 WMAPEVVMCEtmkdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTALDK 255
                       250       260
                ....*....|....*....|....*...
gi 71986426 585 NPSKRlgctgddESASRdIKEHPFFRRI 612
Cdd:cd06644 256 HPETR-------PSAAQ-LLEHPFVSSV 275
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
347-609 6.29e-32

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 125.12  E-value: 6.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKEL-FAIKVLKKDVIIQDDdvecTMTEKRVLALPE-KPSFLVALHScFQTM-DRLY 423
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQ----TLLGKEIKILKElKHENIVALYD-FQEIaNSVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG---------HIKITDFGMC 494
Cdd:cd14202  78 LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 KEnIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELfTAITEHNVSYPKSLSKEA 574
Cdd:cd14202 158 RY-LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDL-RLFYEKNKSLSPNIPRET 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 71986426 575 VSLCKALLiknpskrLGCTGDDESASRDIKE---HPFF 609
Cdd:cd14202 236 SSHLRQLL-------LGLLQRNQKDRMDFDEffhHPFL 266
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
39-90 6.54e-32

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 117.73  E-value: 6.54e-32
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPG 90
Cdd:cd20792   2 HKFVATFFKQPTFCSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKCPG 53
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
347-589 7.08e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 124.47  E-value: 7.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFaikVLKKDVIIQDDDVECTMTEKRVLALPE-KPSFLVALHSCFQTMD-RLYF 424
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQY---VIKKLNLKNASKRERKAAEQEAKLLSKlKHPNIVSYKESFEGEDgFLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQI-QQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFG 500
Cdd:cd08223  78 VMGFCEGGDLYTRLkEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARvlESSSD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATtkTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV-SYPKSLSKEAVSLCK 579
Cdd:cd08223 158 MAT--TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIK 235
                       250
                ....*....|
gi 71986426 580 ALLIKNPSKR 589
Cdd:cd08223 236 AMLHQDPEKR 245
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
346-609 8.31e-32

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: 124.78  E-value: 8.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLkkDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRI--DLEKCQTSMDELRKEIQAMSQCNHPN-VVSYYTSFVVGDELWLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGG---DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMcKENIF--G 500
Cdd:cd06610  78 MPLLSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGV-SASLAtgG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATT---KTFCGTPDYIAPEII-LYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT-------EHNVSYPK- 568
Cdd:cd06610 157 DRTRkvrKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLqndppslETGADYKKy 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71986426 569 -SLSKEAVSLCkalLIKNPSKRlgctgddESASRdIKEHPFF 609
Cdd:cd06610 237 sKSFRKMISLC---LQKDPSKR-------PTAEE-LLKHKFF 267
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
354-609 9.19e-32

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: 125.13  E-value: 9.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKdVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG- 432
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALKKVAL-RKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYMLSSl 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 -DLMYQIQQvgKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGDATTKTF---C 508
Cdd:cd07832  87 sEVLRDEER--PLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR--LFSEEDPRLYshqV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DEL-----------------FTAITEHN-VSYPK 568
Cdd:cd07832 163 ATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDiEQLaivlrtlgtpnektwpeLTSLPDYNkITFPE 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 569 S-----------LSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFF 609
Cdd:cd07832 243 SkgirleeifpdCSPEAIDLLKGLLVYNPKKRLSAE--------EALRHPYF 286
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
348-589 1.40e-31

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 123.82  E-value: 1.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQ-TMDRLYFVM 426
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPN-IVQMFECIEvANGRLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EfVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG-HIKITDFGMCKENIFGDATTK 505
Cdd:cd14164  81 E-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELST 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELftAITEHNVSYPKSLSKEavSLCKALLIK 584
Cdd:cd14164 160 TFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRGVLYPSGVALE--EPCRALIRT 235

                ....*....
gi 71986426 585 ----NPSKR 589
Cdd:cd14164 236 llqfNPSTR 244
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
357-609 2.89e-31

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 123.04  E-value: 2.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  357 GSFGKVLLGEQKTTKELFAIKVLKKDVIIQDddvectmtEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGDLMY 436
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAI--------EPMVHQLMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  437 QIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER-DGHIKITDFGMCKenIFGdaTTKTFCGTPDYIA 515
Cdd:PHA03390  99 LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLCDYGLCK--IIG--TPSCYDGTLDYFS 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  516 PEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDgEDEDELFTAITEH-----NVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:PHA03390 175 PEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK-EDEDEELDLESLLkrqqkKLPFIKNVSKNANDFVQSMLKYNINYRL 253
                        250
                 ....*....|....*....
gi 71986426  591 gCTGDdesasrDIKEHPFF 609
Cdd:PHA03390 254 -TNYN------EIIKHPFL 265
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
354-607 3.49e-31

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: 123.24  E-value: 3.49e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPsfLVALHSCFQTM-------------- 419
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAGFFRRPPPRRKPGALGKP--LDPLDRVYREIailkkldhpnvvkl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 ---------DRLYFVMEFVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITD 490
Cdd:cd14118  80 vevlddpneDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 491 FGMCKENIFGDATTKTFCGTPDYIAPEIIL---YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP 567
Cdd:cd14118 159 FGVSNEFEGDDALLSSTAGTPAFMAPEALSesrKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFP 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71986426 568 KS--LSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHP 607
Cdd:cd14118 239 DDpvVSEQLKDLILRMLDKNPSERITLP--------EIKEHP 272
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
352-589 5.24e-31

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 127.29  E-value: 5.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDD------DVECTMT----------EKRVLALPEKPS--FLVALh 413
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADknraqaEVCCLLNcdffsivkchEDFAKKDPRNPEnvLMIAL- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  414 scfqtmdrlyfVMEFVNGGDLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKIT 489
Cdd:PTZ00283 117 -----------VLDYANAGDLRQEIKSRAKtnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLG 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  490 DFGMCK--ENIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED-EDELFTAITEHNVSY 566
Cdd:PTZ00283 186 DFGFSKmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENmEEVMHKTLAGRYDPL 265
                        250       260
                 ....*....|....*....|...
gi 71986426  567 PKSLSKEAVSLCKALLIKNPSKR 589
Cdd:PTZ00283 266 PPSISPEMQEIVTALLSSDPKRR 288
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
353-592 6.08e-31

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 121.75  E-value: 6.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGg 432
Cdd:cd14082  10 VLGSGQFGIVYGGKHRKTGRDVAIKVIDK-LRFPTKQESQLRNEVAILQQLSHPG-VVNLECMFETPERVFVVMEKLHG- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQI--QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG---HIKITDFGMCKenIFGDAT-TKT 506
Cdd:cd14082  87 DMLEMIlsSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR--IIGEKSfRRS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDgEDEDelftaITE--HNVS--YP----KSLSKEAVSLC 578
Cdd:cd14082 165 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFN-EDED-----INDqiQNAAfmYPpnpwKEISPDAIDLI 238
                       250
                ....*....|....
gi 71986426 579 KALLIKNPSKRLGC 592
Cdd:cd14082 239 NNLLQVKMRKRYSV 252
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
353-590 7.60e-31

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 122.04  E-value: 7.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGE--QKTTKELfAIKVLKKDVIIQDDdvecTMTEKRVLALPE-KPSFLVALHSCFQTMDRLYFVMEFV 429
Cdd:cd14201  13 LVGHGAFAVVFKGRhrKKTDWEV-AIKSINKKNLSKSQ----ILLGKEIKILKElQHENIVALYDVQEMPNSVFLVMEYC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG---------HIKITDFGMCKEnIFG 500
Cdd:cd14201  88 NGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARY-LQS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELfTAITEHN----VSYPKSLSKEAVS 576
Cdd:cd14201 167 NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDL-RMFYEKNknlqPSIPRETSPYLAD 245
                       250
                ....*....|....
gi 71986426 577 LCKALLIKNPSKRL 590
Cdd:cd14201 246 LLLGLLQRNQKDRM 259
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
354-599 7.74e-31

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: 123.06  E-value: 7.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIqdddvectMTEKRVLALP--EKPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEA--------NTQREVAALRlcQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGMCKENIFGDATTKTFC 508
Cdd:cd14180  86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQTPC 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED-------ELFTAITEHNVSYP----KSLSKEAVSL 577
Cdd:cd14180 166 FTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEgeawKGVSEEAKDL 245
                       250       260
                ....*....|....*....|..
gi 71986426 578 CKALLIKNPSKRLGCTGDDESA 599
Cdd:cd14180 246 VRGLLTVDPAKRLKLSELRESD 267
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
348-609 9.58e-31

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 122.04  E-value: 9.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDV--ECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFK---ESEDDEDvkKTALREVKVLRQLRHEN-IVNLKEAFRRKGRLYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVnGGDLMYQIQQVGKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeNIFGDATT 504
Cdd:cd07833  79 FEYV-ERTLLELLEASPGGLPPDAVrSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFAR-ALTARPAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 K--TFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGE-DEDELF-------------TAITEHN---- 563
Cdd:cd07833 157 PltDYVATRWYRAPELLVgDTNYGKPVDVWAIGCIMAELLDGEPLFPGDsDIDQLYliqkclgplppshQELFSSNprfa 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 564 --------------VSYPKSLSKEAVSLCKALLIKNPSKRLGCTGddesasrdIKEHPFF 609
Cdd:cd07833 237 gvafpepsqpesleRRYPGKVSSPALDFLKACLRMDPKERLTCDE--------LLQHPYF 288
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
346-613 1.78e-30

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: 120.91  E-value: 1.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDV-------IIQDDDV--ECTMtekrvlalpekpSFLVALHSCF 416
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIdealqkqILRELDVlhKCNS------------PYIVGFYGAF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCK 495
Cdd:cd06605  69 YSEGDISICMEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 ENIfgDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED------ELFTAITEHNvsyPKS 569
Cdd:cd06605 149 QLV--DSLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEP---PPL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71986426 570 L-----SKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFFRRID 613
Cdd:cd06605 224 LpsgkfSPDFQDFVSQCLQKDPTER--------PSYKELMEHPFIKRYE 264
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
345-589 1.78e-30

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: 120.86  E-value: 1.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYF 424
Cdd:cd13996   5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR--LTEKSSASEKVLREVKALAKLNHPN-IVRYYTAWVEEPPLYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQQVGKFK---EPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDGHIKITDFGMCKE---- 496
Cdd:cd13996  82 QMELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSignq 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 ----------NIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAgqpPFDGEDEDelFTAITE-HNVS 565
Cdd:cd13996 162 krelnnlnnnNNGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMER--STILTDlRNGI 236
                       250       260
                ....*....|....*....|....*...
gi 71986426 566 YPKSLS----KEAvSLCKALLIKNPSKR 589
Cdd:cd13996 237 LPESFKakhpKEA-DLIQSLLSKNPEER 263
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
354-608 2.49e-30

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 120.22  E-value: 2.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVI--IQDDDVECTMTEKRVLALPEKPSfLVALHSCFqtMDRLYF--VMEFV 429
Cdd:cd08222   8 LGSGNFGTVYLVSDLKATADEELKVLKEISVgeLQPDETVDANREAKLLSKLDHPA-IVKFHDSF--VEKESFciVTEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQV----GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLeRDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd08222  85 EGGDLDDKISEYkksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMGTSDLAT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV-SYPKSLSKEAVSLCKALLIK 584
Cdd:cd08222 164 TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRMLNK 243
                       250       260
                ....*....|....*....|....
gi 71986426 585 NPSKRlgctgddESASrDIKEHPF 608
Cdd:cd08222 244 DPALR-------PSAA-EILKIPF 259
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
353-608 2.51e-30

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 120.23  E-value: 2.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGeQKTTKELFAIKVLKKDVIIQDDdvectmTEKRVLALPEKPSFLVALH---------SCFQTmDRLY 423
Cdd:cd06631   8 VLGKGAYGTVYCG-LTSTGQLIAVKQVELDTSDKEK------AEKEYEKLQEEVDLLKTLKhvnivgylgTCLED-NVVS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG----MCKENIF 499
Cdd:cd06631  80 IFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLSS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATT--KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK---SLSKEA 574
Cdd:cd06631 160 GSQSQllKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRlpdKFSPEA 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 71986426 575 VSLCKALLIKNPSKRLgctgddeSASRDIKeHPF 608
Cdd:cd06631 240 RDFVHACLTRDQDERP-------SAEQLLK-HPF 265
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
350-549 3.13e-30

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: 119.91  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   350 FLTVLGKGSFGKV----LLGEQKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFV 425
Cdd:pfam07714   3 LGEKLGEGAFGEVykgtLKGEGENTKIKVAVKTLKEGA--DEEEREDFLEEASIMKKLDHPN-IVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   426 MEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATT 504
Cdd:pfam07714  80 TEYMPGGDLLdFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD-IYDDDYY 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 71986426   505 KTFCGTPD---YIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:pfam07714 159 RKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPG 207
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
348-609 3.27e-30

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: 120.00  E-value: 3.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEkpsfLVALHSCFQTMDRLYFVME 427
Cdd:cd14114   4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPK----LINLHDAFEDDNEMVLILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE--RDGHIKITDFGMCKEnIFGDATT 504
Cdd:cd14114  80 FLSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH-LDPKESV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAIT----EHNVSYPKSLSKEAVSLCKA 580
Cdd:cd14114 159 KVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKscdwNFDDSAFSGISEEAKDFIRK 238
                       250       260
                ....*....|....*....|....*....
gi 71986426 581 LLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14114 239 LLLADPNKRM--------TIHQALEHPWL 259
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
354-590 3.53e-30

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: 120.11  E-value: 3.53e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDD-DVECTMTEKRVLALPE-KPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrGVSREEIEREVNILREiQHPNIITLHDIFENKTDVVLILELVSG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML----ERDGHIKITDFGMCKENIFGDATTKTF 507
Cdd:cd14195  93 GELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKIEAGNEFKNIF 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 cGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV----SYPKSLSKEAVSLCKALLI 583
Cdd:cd14195 173 -GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYdfdeEYFSNTSELAKDFIRRLLV 251

                ....*..
gi 71986426 584 KNPSKRL 590
Cdd:cd14195 252 KDPKKRM 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
353-590 3.64e-30

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: 119.70  E-value: 3.64e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKkDVIIQDDDVECTMtekRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14089   8 VLGLGINGKVLECFHKKTGEKFALKVLR-DNPKARREVELHW---RASGCPHIVRIIDVYENTYQGRKCLLVVMECMEGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQ--VGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENiFGDATTKTF 507
Cdd:cd14089  84 ELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGFAKET-TTKKSLQTP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFdgededelFTA------------ITEHNVSYP----KSLS 571
Cdd:cd14089 163 CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPF--------YSNhglaispgmkkrIRNGQYEFPnpewSNVS 234
                       250
                ....*....|....*....
gi 71986426 572 KEAVSLCKALLIKNPSKRL 590
Cdd:cd14089 235 EEAKDLIRGLLKTDPSERL 253
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
354-589 3.88e-30

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 119.74  E-value: 3.88e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDV-ECTMTekrvLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLrEYNIS----LELSVHPHIIKTYDVAFETEDYYVFAQEYAPYG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQ-QVGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERD-GHIKITDFGMCKENifgDATTKTFCG 509
Cdd:cd13987  77 DLFSIIPpQVG-LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTRRV---GSTVKRVSG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPE---IILYQPY--GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH-----NVSYP---KSLSKEAVS 576
Cdd:cd13987 153 TIPYTAPEvceAKKNEGFvvDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRwqkrkNTAVPsqwRRFTPKALR 232
                       250
                ....*....|...
gi 71986426 577 LCKALLIKNPSKR 589
Cdd:cd13987 233 MFKKLLAPEPERR 245
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
345-608 4.45e-30

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: 119.71  E-value: 4.45e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMtEKRVLA-LPEKPS-------FLVALHSCF 416
Cdd:cd06608   5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD---IIEDEEEEIKL-EINILRkFSNHPNiatfygaFIKKDPPGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QtmDRLYFVMEFVNGG---DLMYQIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG 492
Cdd:cd06608  81 D--DQLWLVMEYCGGGsvtDLVKGLRKKGKrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 493 MCKENifgDATT---KTFCGTPDYIAPEII-----LYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITEH- 562
Cdd:cd06608 159 VSAQL---DSTLgrrNTFIGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIELADGKPPLcDMHPMRALFKIPRNPp 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 71986426 563 -NVSYPKSLSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPF 608
Cdd:cd06608 236 pTLKSPEKWSKEFNDFISECLIKNYEQR--------PFTEELLEHPF 274
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
32-91 5.53e-30

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 112.42  E-value: 5.53e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  32 NVHEIKSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGA 91
Cdd:cd20834   1 KVHEVKGHEFIAKFFRQPTFCSVCKEFLWGFNKQGYQCRQCNAAVHKKCHDKILGKCPGS 60
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
353-561 5.62e-30

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: 119.18  E-value: 5.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKT---TKELFAIKVLKKDviIQDDDVECTMTEKRVLALPEKPsFLVAL-HSCFQTmDRLYFVMEF 428
Cdd:cd00192   2 KLGEGAFGEVYKGKLKGgdgKTVDVAVKTLKED--ASESERKDFLKEARVMKKLGHP-NVVRLlGVCTEE-EPLYLVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDL---------MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeNIF 499
Cdd:cd00192  78 MEGGDLldflrksrpVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSR-DIY 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 500 GDATTKTFCGTPDYI---APEIILYQPYG-KSvDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE 561
Cdd:cd00192 157 DDDYYRKKTGGKLPIrwmAPESLKDGIFTsKS-DVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRK 222
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
348-609 1.10e-29

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: 118.74  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviIQDDDVECTmtekrvlALPE-------KPSFLVALHSCFQTMD 420
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLD--NEEEGIPST-------ALREisllkelKHPNIVKLLDVIHTEN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGgDL-MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniF 499
Cdd:cd07829  72 KLYLVFEYCDQ-DLkKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARA--F 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GdATTKTFcgTPD-----YIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELF---------------- 556
Cdd:cd07829 149 G-IPLRTY--THEvvtlwYRAPEILLgSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEiDQLFkifqilgtpteeswpg 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 557 -TAITEHNVSYPK-----------SLSKEAVSLCKALLIKNPSKRLgctgddeSAsRDIKEHPFF 609
Cdd:cd07829 226 vTKLPDYKPTFPKwpkndlekvlpRLDPEGIDLLSKMLQYNPAKRI-------SA-KEALKHPYF 282
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
347-630 1.16e-29

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: 119.28  E-value: 1.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMtekRVLALPekpsFLVALHSCFQTMDRLYFVM 426
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILL---RYGQHP----NIITLRDVYDDGNSVYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH----IKITDFGMCK----ENi 498
Cdd:cd14091  74 ELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKqlraEN- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 fgdATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF--DGED-EDELFTAITEHNVSYP----KSLS 571
Cdd:cd14091 153 ---GLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFasGPNDtPEVILARIGSGKIDLSggnwDHVS 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 572 KEAVSLCKALLIKNPSKRLgctgddeSASRdIKEHPFFRRIDwfKIETRQIQPPFKPKL 630
Cdd:cd14091 230 DSAKDLVRKMLHVDPSQRP-------TAAQ-VLQHPWIRNRD--SLPQRQLTDPQDAAL 278
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
354-590 1.46e-29

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: 118.18  E-value: 1.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKT--TKELFAIKVLKKDviiqDDDVECTMTEKRVLalpEKPSFLVALHSC--FQTMDRLY------ 423
Cdd:cd13994   1 IGKGATSVVRIVTKKNprSGVLYAVKEYRRR----DDESKRKDYVKRLT---SEYIISSKLHHPniVKVLDLCQdlhgkw 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 -FVMEFVNGGDLMYQIQQVGKF-KEPVAVFYAaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCkeNIFGD 501
Cdd:cd13994  74 cLVMEYCPGGDLFTLIEKADSLsLEEKDCFFK-QILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA--EVFGM 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKT------FCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELF----TAITEHNVSYPK- 568
Cdd:cd13994 151 PAEKEspmsagLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrSAKKSDSAYkayeKSGDFTNGPYEPi 230
                       250       260
                ....*....|....*....|....
gi 71986426 569 --SLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd13994 231 enLLPSECRRLIYRMLHPDPEKRI 254
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
353-551 1.82e-29

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 117.49  E-value: 1.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKttKELFAIKVLKKDViiqDDDVECTM----TEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEF 428
Cdd:cd14061   1 VIGVGGFGKVYRGIWR--GEEVAVKAARQDP---DEDISVTLenvrQEARLFWMLRHPNIIALRGVCLQP-PNLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMyqiQQVGKFKEP--VAVFYAAEIAVGLFFLHSKG---IIYRDLKLDNVML-ERDGH-------IKITDFGMCK 495
Cdd:cd14061  75 ARGGALN---RVLAGRKIPphVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILIlEAIENedlenktLKITDFGLAR 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 496 ENifgDATTK-TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd14061 152 EW---HKTTRmSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGID 205
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
174-278 2.20e-29

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 112.20  E-value: 2.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426    174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDsgcKSKQKTKTLRATLNPQWNETFTYKLLPgDKDRRLSIEVWDWDRT 253
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDP---KEKKKTKVVKNTLNPVWNETFEFEVPP-PELAELEIEVYDKDRF 76
                           90       100
                   ....*....|....*....|....*
gi 71986426    254 SRNDFMGSLSFGISELMKEAASGWY 278
Cdd:smart00239  77 GRDDFIGQVTIPLSDLLLGGRHEKL 101
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
175-280 3.05e-29

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 111.78  E-value: 3.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLIPedsgcKSKQKTKTLRATLNPQWNETFTYKLLPgDKDRRLSIEVWDWDRTS 254
Cdd:cd00030   1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGG-----KQKFKTKVVKNTLNPVWNETFEFPVLD-PESDTLTVEVWDKDRFS 74
                        90       100
                ....*....|....*....|....*...
gi 71986426 255 RNDFMGSLSFGISELMK--EAASGWYKL 280
Cdd:cd00030  75 KDDFLGEVEIPLSELLDsgKEGELWLPL 102
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
354-590 3.61e-29

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: 116.98  E-value: 3.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVI------IQDDDVEctmTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14196  13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgVSREEIE---REVSILRQVLHPN-IITLHDVYENRTDVVLILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG----HIKITDFGMCKEnIFGDAT 503
Cdd:cd14196  89 LVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHE-IEDGVE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSL----SKEAVSLCK 579
Cdd:cd14196 168 FKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFfshtSELAKDFIR 247
                       250
                ....*....|.
gi 71986426 580 ALLIKNPSKRL 590
Cdd:cd14196 248 KLLVKETRKRL 258
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
354-589 4.06e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 116.45  E-value: 4.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd08218   8 IGEGSFGKALLVKSKEDGKQYVIKEINISKM-SPKEREESRKEVAVLSKMKHPN-IVQYQESFEENGNLYIVMDYCDGGD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQI-QQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd08218  86 LYKRInAQRGvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHnvSYP---KSLSKEAVSLCKALLIKNPSK 588
Cdd:cd08218 166 YYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRG--SYPpvpSRYSYDLRSLVSQLFKRNPRD 243

                .
gi 71986426 589 R 589
Cdd:cd08218 244 R 244
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
353-608 4.48e-29

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 116.67  E-value: 4.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVecTMTEKRVLALPEKPSFLVALHScFQTMDRLYFVMEFVNGG 432
Cdd:cd14184   8 VIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL--IENEVSILRRVKHPNIIMLIEE-MDTPAELYLVMELVKGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML----ERDGHIKITDFGMCKeniFGDATTKTFC 508
Cdd:cd14184  85 DLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLAT---VVEGPLYTVC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED--EDELFTAITEHNVSYPK----SLSKEAVSLCKALL 582
Cdd:cd14184 162 GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSpywdNITDSAKELISHML 241
                       250       260
                ....*....|....*....|....*.
gi 71986426 583 IKNPSKRlgCTGDdesasrDIKEHPF 608
Cdd:cd14184 242 QVNVEAR--YTAE------QILSHPW 259
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
361-589 4.53e-29

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 121.28  E-value: 4.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  361 KVLLGEQKTTKELFAI-------KVLKKDVIIQDDDvECTMTEKRVLALPEKPSFLVALH-SCFQTMDRLYFVMEFVNGG 432
Cdd:PTZ00267  72 TTLVGRNPTTAAFVATrgsdpkeKVVAKFVMLNDER-QAAYARSELHCLAACDHFGIVKHfDDFKSDDKLLLIMEYGSGG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  433 DLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDATT---- 504
Cdd:PTZ00267 151 DLNKQIKQRLKehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQ--YSDSVSldva 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  505 KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS-YPKSLSKEAVSLCKALLI 583
Cdd:PTZ00267 229 SSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLS 308

                 ....*.
gi 71986426  584 KNPSKR 589
Cdd:PTZ00267 309 KNPALR 314
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
347-608 6.16e-29

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: 116.68  E-value: 6.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiQDDDVectmTEKRVLALPE-KPSFLVALHSCFQTMDRLYFV 425
Cdd:cd06645  12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPG-EDFAV----VQQEIIMMKDcKHSNIVAYFGSYLRRDKLWIC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd06645  87 MEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQ---PYGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTaITEHNVSYPKSLSKEAVS----- 576
Cdd:cd06645 167 SFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFL-MTKSNFQPPKLKDKMKWSnsfhh 245
                       250       260       270
                ....*....|....*....|....*....|..
gi 71986426 577 LCKALLIKNPSKRlgctgddeSASRDIKEHPF 608
Cdd:cd06645 246 FVKMALTKNPKKR--------PTAEKLLQHPF 269
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
349-610 6.48e-29

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 117.06  E-value: 6.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 349 NFLTVlGKGSFGKVLLGEQKTTKELFAIKvlKKDVIIQDDDvECTMTEKrVLALPEKPSFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd06658  26 SFIKI-GEGSTGIVCIATEKHTGKQVAVK--KMDLRKQQRR-ELLFNEV-VIMRDYHHENVVDMYNSYLVGDELWVVMEF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFC 508
Cdd:cd06658 101 LEGGALTDIVTHTRMNEEQIATV-CLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLV 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSL---CKALLIKN 585
Cdd:cd06658 180 GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLrgfLDLMLVRE 259
                       250       260
                ....*....|....*....|....*
gi 71986426 586 PSKRlgctgddeSASRDIKEHPFFR 610
Cdd:cd06658 260 PSQR--------ATAQELLQHPFLK 276
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
349-611 8.08e-29

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 116.66  E-value: 8.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 349 NFLTVlGKGSFGKVLLGEQKTTKELFAIKvlKKDVIIQDDDvECTMTEKrVLALPEKPSFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd06657  24 NFIKI-GEGSTGIVCIATVKSSGKLVAVK--KMDLRKQQRR-ELLFNEV-VIMRDYQHENVVEMYNSYLVGDELWVVMEF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAeIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFC 508
Cdd:cd06657  99 LEGGALTDIVTHTRMNEEQIAAVCLA-VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSL---CKALLIKN 585
Cdd:cd06657 178 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLkgfLDRLLVRD 257
                       250       260
                ....*....|....*....|....*.
gi 71986426 586 PSKRlgctgddeSASRDIKEHPFFRR 611
Cdd:cd06657 258 PAQR--------ATAAELLKHPFLAK 275
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
353-608 8.39e-29

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 115.86  E-value: 8.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVecTMTEKRVLALPEKPSFLVALHScFQTMDRLYFVMEFVNGG 432
Cdd:cd14183  13 TIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM--IQNEVSILRRVKHPNIVLLIEE-MDMPTELYLVMELVKGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML--ERDGH--IKITDFGMCKeniFGDATTKTFC 508
Cdd:cd14183  90 DLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSksLKLGDFGLAT---VVDGPLYTVC 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDG--EDEDELFTAITEHNVSYP----KSLSKEAVSLCKALL 582
Cdd:cd14183 167 GTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFPspywDNVSDSAKELITMML 246
                       250       260
                ....*....|....*....|....*.
gi 71986426 583 IKNPSKRLgctgddesASRDIKEHPF 608
Cdd:cd14183 247 QVDVDQRY--------SALQVLEHPW 264
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
353-610 9.62e-29

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 116.87  E-value: 9.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDD--DVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd14094  10 VIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHP-HIVELLETYSSDGMLYMVFEFMD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd14094  89 GADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDeLFTAITEHNVSY----PKSLSKEAVSLCK 579
Cdd:cd14094 169 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMnprqWSHISESAKDLVR 247
                       250       260       270
                ....*....|....*....|....*....|.
gi 71986426 580 ALLIKNPSKRLGCTgddesasrDIKEHPFFR 610
Cdd:cd14094 248 RMLMLDPAERITVY--------EALNHPWIK 270
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
357-609 2.51e-28

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 114.57  E-value: 2.51e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 357 GSFGKVLLGEQKTTKELFAIKVLKKDViiqdddvECTMTEKRVLalPEKPSFLVALHSCFQTMDRLYFVMEFVNGGDLMY 436
Cdd:cd05576  10 GVIDKVLLVMDTRTQETFILKGLRKSS-------EYSRERKTII--PRCVPNMVCLRKYIISEESVFLVLQHAEGGKLWS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 437 QIQQVGKFKEPVAVF----------------------YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC 494
Cdd:cd05576  81 YLSKFLNDKEIHQLFadlderlaaasrfyipeeciqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 KE---NIFGDATTKTFCgtpdyiAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDedelfTAITEH-NVSYPKSL 570
Cdd:cd05576 161 SEvedSCDSDAIENMYC------APEVGGISEETEACDWWSLGALLFELLTGKALVECHP-----AGINTHtTLNIPEWV 229
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71986426 571 SKEAVSLCKALLIKNPSKRLGCtgdDESASRDIKEHPFF 609
Cdd:cd05576 230 SEEARSLLQQLLQFNPTERLGA---GVAGVEDIKSHPFF 265
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
353-609 2.54e-28

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 114.26  E-value: 2.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQ----DDDVECTMtEKRVLALPEKPS--FLVALHSCFQTMDRLYFVM 426
Cdd:cd14005   7 LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEwamiNGPVPVPL-EIALLLKASKPGvpGVIRLLDWYERPDGFLLIM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EF-VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDGHIKITDFGmCKEnIFGDATT 504
Cdd:cd14005  86 ERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFG-CGA-LLKDSVY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEdelftaITEHNVSYPKSLSKEAVSLCKALLI 583
Cdd:cd14005 164 TDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFENDEQ------ILRGNVLFRPRLSKECCDLISRCLQ 237
                       250       260
                ....*....|....*....|....*.
gi 71986426 584 KNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14005 238 FDPSKRP--------SLEQILSHPWF 255
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
354-590 2.67e-28

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: 113.92  E-value: 2.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKT-TKELFAIKVLKKDVIIQDDdVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14121   3 LGSGTYATVYKAYRKSgAREVVAVKCVSKSSLNKAS-TENLLTEIELLKKLKHP-HIVELKDFQWDEEHIYLIMEYCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG--HIKITDFGMCKeNIFGDATTKTFCGT 510
Cdd:cd14121  81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQ-HLKPNDEAHSLRGS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHN-VSYPKS--LSKEAVSLCKALLIKNPS 587
Cdd:cd14121 160 PLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQRDPD 239

                ...
gi 71986426 588 KRL 590
Cdd:cd14121 240 RRI 242
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
354-610 3.69e-28

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 113.87  E-value: 3.69e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVL------KKDVIIQDDDVectMTEKRvlalpeKPSFLVALHScFQTMDRLYFVME 427
Cdd:cd06647  15 IGQGASGTVYTAIDVATGQEVAIKQMnlqqqpKKELIINEILV---MRENK------NPNIVNYLDS-YLVGDELWVVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVgKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTF 507
Cdd:cd06647  85 YLAGGSLTDVVTET-CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH---NVSYPKSLSkeavSLCKALLik 584
Cdd:cd06647 164 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLS----AIFRDFL-- 237
                       250       260
                ....*....|....*....|....*.
gi 71986426 585 npSKRLGCTGDDESASRDIKEHPFFR 610
Cdd:cd06647 238 --NRCLEMDVEKRGSAKELLQHPFLK 261
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
355-608 4.62e-28

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: 113.94  E-value: 4.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 355 GKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDD---VECTMTEKRVLALPEKPSFL----VALHScfqtmDRLYFVME 427
Cdd:cd06626   9 GEGTFGKVYTAVNLDTGELMAMKEIR----FQDNDpktIKEIADEMKVLEGLDHPNLVryygVEVHR-----EEVYIFME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGDATTKTF 507
Cdd:cd06626  80 YCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAV--KLKNNTTTMA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 C-------GTPDYIAPEIILYQP---YGKSVDWWAYGVLLFEMLAGQPPFDgEDEDE---LFTAITEHNVSYPKSL--SK 572
Cdd:cd06626 158 PgevnslvGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWS-ELDNEwaiMYHVGMGHKPPIPDSLqlSP 236
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 573 EAVSLCKALLIKNPSKRlgctgddESASrDIKEHPF 608
Cdd:cd06626 237 EGKDFLSRCLESDPKKR-------PTAS-ELLDHPF 264
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
353-608 6.74e-28

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 113.27  E-value: 6.74e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIK-VLKKDviiqDDDVECTMTEkrvlalpekpsflVALHS------------CFQTM 419
Cdd:cd06624  15 VLGKGTFGVVYAARDLSTQVRIAIKeIPERD----SREVQPLHEE-------------IALHSrlshknivqylgSVSED 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 DRLYFVMEFVNGGDLMYQIQQVG---KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER-DGHIKITDFGMCK 495
Cdd:cd06624  78 GFFKIFMEQVPGGSLSALLRSKWgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 ENIFGDATTKTFCGTPDYIAPEIILYQP--YGKSVDWWAYGVLLFEMLAGQPPF--DGEDEDELFTA--ITEHNvSYPKS 569
Cdd:cd06624 158 RLAGINPCTETFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFieLGEPQAAMFKVgmFKIHP-EIPES 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71986426 570 LSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPF 608
Cdd:cd06624 237 LSEEAKSFILRCFEPDPDKR--------ATASDLLQDPF 267
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
354-608 7.47e-28

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 113.58  E-value: 7.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILASCDHP-NIVKLLDAFYYENNLWILIEFCAGGA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 L---MYQIQQvgKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd06643  89 VdavMLELER--PLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQ-----PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH---NVSYPKSLSKEAVSLCKALL 582
Cdd:cd06643 167 PYWMAPEVVMCEtskdrPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSeppTLAQPSRWSPEFKDFLRKCL 246
                       250       260
                ....*....|....*....|....*.
gi 71986426 583 IKNPSKRLGCTgddesasrDIKEHPF 608
Cdd:cd06643 247 EKNVDARWTTS--------QLLQHPF 264
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
353-551 7.63e-28

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 113.20  E-value: 7.63e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKttKELFAIKVLKKDviiQDDDVECTM----TEKRVLALPEKPSFLVALHSCFQTMDrLYFVMEF 428
Cdd:cd14147  10 VIGIGGFGKVYRGSWR--GELVAVKAARQD---PDEDISVTAesvrQEARLFAMLAHPNIIALKAVCLEEPN-LCLVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIqqVGKFKEP-VAVFYAAEIAVGLFFLHSKGI---IYRDLKLDNVMLERDGH--------IKITDFGMCKE 496
Cdd:cd14147  84 AAGGPLSRAL--AGRRVPPhVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehktLKITDFGLARE 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 497 niFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd14147 162 --WHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGID 214
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
354-593 7.92e-28

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 112.79  E-value: 7.92e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEkpsfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14191  10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPK----LVQCVDAFEEKANIVMVLEMVSGGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LERDG-HIKITDFGMCKEnIFGDATTKTFCGT 510
Cdd:cd14191  86 LFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARR-LENAGSLKVLFGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCKALLIKNP 586
Cdd:cd14191 165 PEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDM 244

                ....*..
gi 71986426 587 SKRLGCT 593
Cdd:cd14191 245 KARLTCT 251
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
353-547 1.03e-27

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: 113.01  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKvlkkDVIIQDDDVECTMTEKRVL-ALPEKPSFLVALH--------SCFQTMDRLY 423
Cdd:cd06628   7 LIGSGSFGSVYLGMNASSGELMAVK----QVELPSVSAENKDRKKSMLdALQREIALLRELQhenivqylGSSSDANHLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE---NIFG 500
Cdd:cd06628  83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleaNSLS 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATTK---TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd06628 163 TKNNGarpSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF 212
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
354-610 1.17e-27

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 113.66  E-value: 1.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSFLVALHScFQTMDRLYFVMEFVNGGD 433
Cdd:cd06656  27 IGQGASGTVYTAIDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDS-YLVGDELWVVMEYLAGGS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPDY 513
Cdd:cd06656 103 LTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 514 IAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVsyPKSLSKEAVSlckALLIKNPSKRLGCT 593
Cdd:cd06656 182 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT--PELQNPERLS---AVFRDFLNRCLEMD 256
                       250
                ....*....|....*..
gi 71986426 594 GDDESASRDIKEHPFFR 610
Cdd:cd06656 257 VDRRGSAKELLQHPFLK 273
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
348-611 1.45e-27

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 112.84  E-value: 1.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLkkDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd06642   6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKII--DLEEAEDEIEDIQQEITVLSQCDSP-YITRYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTF 507
Cdd:cd06642  83 YLGGGSAL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd06642 162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNsDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDP 241
                       250       260
                ....*....|....*....|....*
gi 71986426 587 SKRlgctgddeSASRDIKEHPFFRR 611
Cdd:cd06642 242 RFR--------PTAKELLKHKFITR 258
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
347-589 1.60e-27

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: 112.43  E-value: 1.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVecTMTEKRVLALPE-KPSFLVALHSCFQTMDRLYFV 425
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLE---PGDDF--SLIQQEIFMVKEcKHCNIVAYFGSYLSREKLWIC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd06646  85 MEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQP---YGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTaITEHNVSYPKSLSKEAVS----- 576
Cdd:cd06646 165 SFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFL-MSKSNFQPPKLKDKTKWSstfhn 243
                       250
                ....*....|...
gi 71986426 577 LCKALLIKNPSKR 589
Cdd:cd06646 244 FVKISLTKNPKKR 256
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
162-280 1.79e-27

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 107.33  E-value: 1.79e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 162 GRLRIEA--HIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPeDSGCKSKQKTKTLRATLNPQWNETFTYKLLPGD- 238
Cdd:cd04031   3 GRIQIQLwyDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLP-DRSEKSKRRTKTVKKTLNPEWNQTFEYSNVRREt 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71986426 239 -KDRRLSIEVWDWDRTSRNDFMGSLSFGISELMKEAASGWYKL 280
Cdd:cd04031  82 lKERTLEVTVWDYDRDGENDFLGEVVIDLADALLDDEPHWYPL 124
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
354-609 1.99e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 112.77  E-value: 1.99e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd06659  29 IGEGSTGVVCIAREKHSGRQVAVKMMD---LRKQQRRELLFNEVVIMRDYQHPN-VVEMYKSYLVGEELWVLMEYLQGGA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVgLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATT-KTFCGTPD 512
Cdd:cd06659 105 LTDIVSQTRLNEEQIATVCEAVLQA-LAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQ-ISKDVPKrKSLVGTPY 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSL---CKALLIKNPSKR 589
Cdd:cd06659 183 WMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVLrdfLERMLVRDPQER 262
                       250       260
                ....*....|....*....|
gi 71986426 590 lgctgddeSASRDIKEHPFF 609
Cdd:cd06659 263 --------ATAQELLDHPFL 274
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
348-611 2.57e-27

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 112.09  E-value: 2.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLkkDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKII--DLEEAEDEIEDIQQEITVLSQCDSP-YVTKYYGSYLKDTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTF 507
Cdd:cd06641  83 YLGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*F 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV-----SYPKSLsKEAVSLCkalL 582
Cdd:cd06641 162 VGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPptlegNYSKPL-KEFVEAC---L 237
                       250       260
                ....*....|....*....|....*....
gi 71986426 583 IKNPSKRlgctgddeSASRDIKEHPFFRR 611
Cdd:cd06641 238 NKEPSFR--------PTAKELLKHKFILR 258
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
348-589 3.22e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 112.01  E-value: 3.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd07848   3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFK-DSEENEEVKETTLRELKMLRTLKQEN-IVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGgDLMYQIQQVGKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG-DATTK 505
Cdd:cd07848  81 YVEK-NMLELLEEMPNGVPPEKVrSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGsNANYT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELFT-----------------------AITE 561
Cdd:cd07848 160 EYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEiDQLFTiqkvlgplpaeqmklfysnprfhGLRF 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 562 HNVSYPKSLSKE--------AVSLCKALLIKNPSKR 589
Cdd:cd07848 240 PAVNHPQSLERRylgilsgvLLDLMKNLLKLNPTDR 275
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
104-153 3.56e-27

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 103.90  E-value: 3.56e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20793   1 HKFKVHTYYSPTFCDHCGSLLYGLVRQGLKCKDCGMNVHHRCKENVPHLC 50
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
354-608 4.57e-27

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 111.58  E-value: 4.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVL-KKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTM------------- 419
Cdd:cd14200   8 IGKGSYGVVKLAYNESDDKYYAMKVLsKKKLLKQYGFPRRPPPRGSKAAQGEQAKPLAPLERVYQEIailkkldhvnivk 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 ----------DRLYFVMEFVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKIT 489
Cdd:cd14200  88 lievlddpaeDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 490 DFGMCKENIFGDATTKTFCGTPDYIAPEIIL--YQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSY 566
Cdd:cd14200 167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLSdsGQSFsGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEF 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71986426 567 PK--SLSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPF 608
Cdd:cd14200 247 PEepEISEELKDLILKMLDKNPETRITVP--------EIKVHPW 282
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
353-593 5.37e-27

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 110.85  E-value: 5.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKkDVIIQDDDVECTMtekRVLALPEkpsfLVALHSCFQTMDR----LYFVMEF 428
Cdd:cd14172  11 VLGLGVNGKVLECFHRRTGQKCALKLLY-DSPKARREVEHHW---RASGGPH----IVHILDVYENMHHgkrcLLIIMEC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd14172  83 MEGGELFSRIQERGDqaFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNAL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 tKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH----NVSYPK----SLSKEAV 575
Cdd:cd14172 163 -QTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRirmgQYGFPNpewaEVSEEAK 241
                       250
                ....*....|....*...
gi 71986426 576 SLCKALLIKNPSKRLGCT 593
Cdd:cd14172 242 QLIRHLLKTDPTERMTIT 259
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
354-610 6.65e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 111.35  E-value: 6.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVL------LGEQKTTKELFAIKVLKKDVIIQDddvectmtekrVLALPE-KPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd06655  27 IGQGASGTVFtaidvaTGQEVAIKQINLQKQPKKELIINE-----------ILVMKElKNPNIVNFLDSFLVGDELFVVM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPVAVFyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKT 506
Cdd:cd06655  96 EYLAGGSLTDVVTETCMDEAQIAAV-CRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRST 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH---NVSYPKSLSKEAVSLCKALLI 583
Cdd:cd06655 175 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLSPIFRDFLNRCLE 254
                       250       260
                ....*....|....*....|....*..
gi 71986426 584 KNPSKRlgctgddeSASRDIKEHPFFR 610
Cdd:cd06655 255 MDVEKR--------GSAKELLQHPFLK 273
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
353-609 7.68e-27

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: 110.83  E-value: 7.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLK----KDVIIQDDDV-ECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVME 427
Cdd:cd14181  17 VIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVrSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVFD 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLM-YQIQQVG-KFKEPVAVFYAAEIAVglFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGM-CkeNIFGDATT 504
Cdd:cd14181  97 LMRRGELFdYLTEKVTlSEKETRSIMRSLLEAV--SYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsC--HLEPGEKL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEII------LYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE--HNVSYPK--SLSKEA 574
Cdd:cd14181 173 RELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEgrYQFSSPEwdDRSSTV 252
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71986426 575 VSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14181 253 KDLISRLLVVDPEIRL--------TAEQALQHPFF 279
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
354-551 7.97e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 110.97  E-value: 7.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSFLVALHScFQTMDRLYFVMEFVNGGD 433
Cdd:cd06654  28 IGQGASGTVYTAMDVATGQEVAIRQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDS-YLVGDELWVVMEYLAGGS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTPDY 513
Cdd:cd06654 104 LTDVVTETCMDEGQIAAV-CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 182
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 71986426 514 IAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd06654 183 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 220
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
353-589 1.00e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 109.82  E-value: 1.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDvECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd08220   7 VVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEER-QAALNEVKVLSMLHHPN-IIEYYESFLEDKALMIVMEYAPGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI-KITDFGMCKEnIFGDATTKTFCG 509
Cdd:cd08220  85 TLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKI-LSSKSKAYTVVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS-YPKSLSKEAVSLCKALLIKNPSK 588
Cdd:cd08220 164 TPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHLDPNK 243

                .
gi 71986426 589 R 589
Cdd:cd08220 244 R 244
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
174-267 1.06e-26

C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176030 [Multi-domain]  Cd Length: 133  Bit Score: 105.51  E-value: 1.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPeDSGCKSKQKTKTLRATLNPQWNETFTYKLLPGDKDRR-LSIEVWDWDR 252
Cdd:cd08384  14 GLIVGIIRCVNLAAMDANGYSDPFVKLYLKP-DAGKKSKHKTQVKKKTLNPEFNEEFFYDIKHSDLAKKtLEITVWDKDI 92
                        90
                ....*....|....*
gi 71986426 253 TSRNDFMGSLSFGIS 267
Cdd:cd08384  93 GKSNDYIGGLQLGIN 107
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
348-546 1.28e-26

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 110.14  E-value: 1.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLkkDVIIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVME 427
Cdd:cd06640   6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKII--DLEEAEDEIEDIQQEITVLSQCDSP-YVTKYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTF 507
Cdd:cd06640  83 YLGGGSAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPP 546
Cdd:cd06640 162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
353-611 1.37e-26

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: 110.00  E-value: 1.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVL--KKDVIIQDDDV----ECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd14182  10 ILGRGVSSVVRRCIHKPTRQEYAVKIIdiTGGGSFSPEEVqelrEATLKEIDILRKVSGHPNIIQLKDTYETNTFFFLVF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVgLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDATTK 505
Cdd:cd14182  90 DLMKKGELFdYLTEKVTLSEKETRKIMRALLEV-ICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPGEKLR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIIL------YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSY--PK--SLSKEAV 575
Cdd:cd14182 168 EVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPEwdDRSDTVK 247
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 576 SLCKALLIKNPSKRLgctgddesASRDIKEHPFFRR 611
Cdd:cd14182 248 DLISRFLVVQPQKRY--------TAEEALAHPFFQQ 275
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
354-608 1.91e-26

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 109.67  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQD-----------------------DDVECTMTEKRVLALPEKPSfLV 410
Cdd:cd14199  10 IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQagfprrppprgaraapegctqprGPIERVYQEIAILKKLDHPN-VV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 411 ALHSCFQ--TMDRLYFVMEFVNGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI 488
Cdd:cd14199  89 KLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKI 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 489 TDFGMCKENIFGDATTKTFCGTPDYIAPEIILYQP---YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS 565
Cdd:cd14199 168 ADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRkifSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQPLE 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 71986426 566 YPK--SLSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPF 608
Cdd:cd14199 248 FPDqpDISDDLKDLLFRMLDKNPESRISVP--------EIKLHPW 284
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
354-567 2.80e-26

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: 107.97  E-value: 2.80e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTtkELFAIKVLKKDviiqdddvecTMTEKRVLALPEKPSFLVALHSCFQTmdRLY-FVMEFVNGG 432
Cdd:cd14059   1 LGSGAQGAVFLGKFRG--EEVAVKKVRDE----------KETDIKHLRKLNHPNIIKFKGVCTQA--PCYcILMEYCPYG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLmYQIQQVGKFKEP-VAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDATTK-TFCGT 510
Cdd:cd14059  67 QL-YEVLRAGREITPsLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKE--LSEKSTKmSFAGT 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP 567
Cdd:cd14059 144 VAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLP 200
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
353-594 3.04e-26

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 108.51  E-value: 3.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEkpsfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14192  11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVN----LIQLYDAFESKTNLTLIMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LERDGH-IKITDFGMCKENIFGDATTKTFcG 509
Cdd:cd14192  87 ELFDRItDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVNF-G 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCKALLIKN 585
Cdd:cd14192 166 TPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVKE 245

                ....*....
gi 71986426 586 PSKRLGCTG 594
Cdd:cd14192 246 KSCRMSATQ 254
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
174-277 3.35e-26

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 105.10  E-value: 3.35e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGcKSKQKTKTLRATLNPQWNETFTYKLL-PGD-KDRRLSIEVWDWD 251
Cdd:cd04020  28 ELHVWVKEAKNLPALKSGGTSDSFVKCYLLPDKSK-KSKQKTPVVKKSVNPVWNHTFVYDGVsPEDlSQACLELTVWDHD 106
                        90       100
                ....*....|....*....|....*..
gi 71986426 252 RTSRNDFMGSLSFGISELM-KEAASGW 277
Cdd:cd04020 107 KLSSNDFLGGVRLGLGTGKsYGQAVDW 133
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
351-609 4.60e-26

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: 108.52  E-value: 4.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAikvLKKDVIIQDDDVECTMTEKRVLALPEKPSF----LVALHSCFQTMDR----- 421
Cdd:cd07838   4 VAEIGEGAYGTVYKARDLQDGRFVA---LKKVRVPLSEEGIPLSTIREIALLKQLESFehpnVVRLLDVCHGPRTdrelk 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNGgDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIF 499
Cdd:cd07838  81 LTLVFEHVDQ-DLATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLAR--IY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATTKTFC-GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE----DELFTAI---TEH----NVSYP 567
Cdd:cd07838 158 SFEMALTSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlGKIFDVIglpSEEewprNSALP 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 568 KS----------------LSKEAVSLCKALLIKNPSKRLGctgddesaSRDIKEHPFF 609
Cdd:cd07838 238 RSsfpsytprpfksfvpeIDEEGLDLLKKMLTFNPHKRIS--------AFEALQHPYF 287
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
347-561 4.78e-26

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 107.97  E-value: 4.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTT-KELFAIK-------VLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQT 418
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSNgQTLLALKeinmtnpAFGRTEQERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 MDRLYFVMEFVNG---GDLMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLH-SKGIIYRDLKLDNVMLERDGHIKITDFGM 493
Cdd:cd08528  81 NDRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 494 CKENIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd08528 161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVE 228
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
353-610 6.15e-26

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: 108.19  E-value: 6.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVectMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14174   9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRV---FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE---RDGHIKITDF----GMCKENIFGDATT- 504
Cdd:cd14174  86 SILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCEspdKVSPVKICDFdlgsGVKLNSACTPITTp 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 --KTFCGTPDYIAPEII-LYQP----YGKSVDWWAYGVLLFEMLAGQPPFDGE---------------DEDELFTAITEH 562
Cdd:cd14174 166 elTTPCGSAEYMAPEVVeVFTDeatfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFESIQEG 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 563 NVSYPKS----LSKEAVSLCKALLIKNPSKRLgctgddeSASRdIKEHPFFR 610
Cdd:cd14174 246 KYEFPDKdwshISSEAKDLISKLLVRDAKERL-------SAAQ-VLQHPWVQ 289
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
345-593 7.18e-26

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 107.31  E-value: 7.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLT--VLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRL 422
Cdd:cd14190   1 SSTFSIHSkeVLGGGKFGKVHTCTEKRTGLKLAAKVINKQ---NSKDKEMVLLEIQVMNQLNHRN-LIQLYEAIETPNEI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERDGH-IKITDFGMCKENIF 499
Cdd:cd14190  77 VLFMEYVEGGELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATTKTFcGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAV 575
Cdd:cd14190 157 REKLKVNF-GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAK 235
                       250
                ....*....|....*...
gi 71986426 576 SLCKALLIKNPSKRLGCT 593
Cdd:cd14190 236 DFVSNLIIKERSARMSAT 253
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
353-608 9.51e-26

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 106.92  E-value: 9.51e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLalpeKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14193  11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQL----NHANLIQLYDAFESRNDIVLVMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LERDGH-IKITDFGMCKENIFGDATTKTFcG 509
Cdd:cd14193  87 ELFDRIiDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLRVNF-G 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCKALLIKN 585
Cdd:cd14193 166 TPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEEAKDFISKLLIKE 245
                       250       260
                ....*....|....*....|...
gi 71986426 586 PSKRLgctgddeSASRDIKeHPF 608
Cdd:cd14193 246 KSWRM-------SASEALK-HPW 260
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
347-589 1.02e-25

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: 106.70  E-value: 1.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVM 426
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPN-IVRYYSSWEEGGHLYIQM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGG---DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE-NIFGDA 502
Cdd:cd13997  80 ELCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRlETSGDV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTktfcGTPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQP-PFDGEDEDELFTAItehnVSYP--KSLSKEAVSLC 578
Cdd:cd13997 160 EE----GDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEPlPRNGQQWQQLRQGK----LPLPpgLVLSQELTRLL 231
                       250
                ....*....|.
gi 71986426 579 KALLIKNPSKR 589
Cdd:cd13997 232 KVMLDPDPTRR 242
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
350-589 1.10e-25

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: 107.05  E-value: 1.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKD--VIIQDDDVECT--MTEKRVLALPEKPSFLVALHSCFQTMDRLYFV 425
Cdd:cd13993   4 LISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpNSKDGNDFQKLpqLREIDLHRRVSRHPNIITLHDVFETEVAIYIV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQI----QQVGKFKEPVAVFyaAEIAVGLFFLHSKGIIYRDLKLDNVMLERD-GHIKITDFGMckenifg 500
Cdd:cd13993  84 LEYCPNGDLFEAItenrIYVGKTELIKNVF--LQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGL------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 dATTKTF-----CGTPDYIAPEII-----LYQPYG-KSVDWWAYGVLLFEMLAGQPPFDGEDE-DELFTAITEHNVSYPK 568
Cdd:cd13993 155 -ATTEKIsmdfgVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPWKIASEsDPIFYDYYLNSPNLFD 233
                       250       260
                ....*....|....*....|....
gi 71986426 569 S---LSKEAVSLCKALLIKNPSKR 589
Cdd:cd13993 234 VilpMSDDFYNLLRQIFTVNPNNR 257
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
353-608 1.49e-25

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: 107.04  E-value: 1.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVectMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14173   9 VLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRV---FREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI---KITDFGM---CKENifGDATT-- 504
Cdd:cd14173  86 SILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLgsgIKLN--SDCSPis 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 ----KTFCGTPDYIAPEII-----LYQPYGKSVDWWAYGVLLFEMLAGQPPFDGE-------DEDE--------LFTAIT 560
Cdd:cd14173 164 tpelLTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEacpacqnmLFESIQ 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 561 EHNVSYPKS----LSKEAVSLCKALLIKNPSKRLgctgddeSASRdIKEHPF 608
Cdd:cd14173 244 EGKYEFPEKdwahISCAAKDLISKLLVRDAKQRL-------SAAQ-VLQHPW 287
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
354-623 2.57e-25

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: 106.65  E-value: 2.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtmtekrVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14175   9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEI------LLRYGQHPN-IITLKDVYDDGKHVYLVTELMRGGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LERDGH---IKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd14175  82 LLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED---ELFTAITEHNVSYP----KSLSKEAVSLCKALL 582
Cdd:cd14175 162 TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDtpeEILTRIGSGKFTLSggnwNTVSDAAKDLVSKML 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71986426 583 IKNPSKRLgctgddesASRDIKEHPFFRRIDwfKIETRQIQ 623
Cdd:cd14175 242 HVDPHQRL--------TAKQVLQHPWITQKD--KLPQSQLN 272
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
347-567 2.98e-25

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 105.89  E-value: 2.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLT---VLGKGSFGKV---LLGEQKTtkelfAIKVLKKDviiQDDDVECTM----TEKRVLALPEKPSFLVALHSCF 416
Cdd:cd14145   4 DFSELVleeIIGIGGFGKVyraIWIGDEV-----AVKAARHD---PDEDISQTIenvrQEAKLFAMLKHPNIIALRGVCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDrLYFVMEFVNGGDLMYQIQqvGKFKEP-VAVFYAAEIAVGLFFLHSKGI---IYRDLKLDNVM-LER-------DG 484
Cdd:cd14145  76 KEPN-LCLVMEFARGGPLNRVLS--GKRIPPdILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILiLEKvengdlsNK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 485 HIKITDFGMCKEniFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNV 564
Cdd:cd14145 153 ILKITDFGLARE--WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKL 230

                ...
gi 71986426 565 SYP 567
Cdd:cd14145 231 SLP 233
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
353-551 4.37e-25

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 105.12  E-value: 4.37e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKelFAIKVLKKDviiQDDDVECTM----TEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEF 428
Cdd:cd14146   1 IIGVGGFGKVYRATWKGQE--VAVKAARQD---PDEDIKATAesvrQEAKLFSMLRHPN-IIKLEGVCLEEPNLCLVMEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEP---------VAVFYAAEIAVGLFFLHSKG---IIYRDLKLDNVML-ERDGH-------IKI 488
Cdd:cd14146  75 ARGGTLNRALAAANAAPGPrrarripphILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLlEKIEHddicnktLKI 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986426 489 TDFGMCKEniFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd14146 155 TDFGLARE--WHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGID 215
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
353-547 4.80e-25

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: 105.11  E-value: 4.80e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPE-KPSFLVALHSCFQ--TMDRLYFVMEFV 429
Cdd:cd06653   9 LLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALECEIQLLKNlRHDRIVQYYGCLRdpEEKKLSIFVEYM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFGDAT-TKT 506
Cdd:cd06653  89 PGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriQTICMSGTgIKS 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd06653 169 VTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
348-589 4.98e-25

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: 104.90  E-value: 4.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL-----KKDVIIQDDDVECTMTEKRVLALpekpsflvalHSCFQTMDRL 422
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqaeEKQGVLQEYEILKSLHHERIMAL----------HEAYITPRYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE-NIFGD 501
Cdd:cd14111  75 VLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSfNPLSL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS----YPKsLSKEAVSL 577
Cdd:cd14111 155 RQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDafklYPN-VSQSASLF 233
                       250
                ....*....|..
gi 71986426 578 CKALLIKNPSKR 589
Cdd:cd14111 234 LKKVLSSYPWSR 245
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
354-589 5.46e-25

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: 104.67  E-value: 5.46e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDdvecTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQ----VTHELGVLQSLQHPQ-LVGLLDTFETPTSYILVLEMADQGR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGmckenifgDA----TT-- 504
Cdd:cd14113  90 LLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFG--------DAvqlnTTyy 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 -KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCK 579
Cdd:cd14113 162 iHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVC 241
                       250
                ....*....|
gi 71986426 580 ALLIKNPSKR 589
Cdd:cd14113 242 FLLQMDPAKR 251
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
354-590 7.48e-25

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 105.24  E-value: 7.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVL---KK--------------DVIIQDDDVECTMtekrvLALPEKPSflvalhscf 416
Cdd:cd14171  14 LGTGISGPVRVCVKKSTGERFALKILldrPKartevrlhmmcsghPNIVQIYDVYANS-----VQFPGESS--------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 qTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER---DGHIKITDFGM 493
Cdd:cd14171  80 -PRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDnseDAPIKLCDFGF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 494 CKENIfGDATTKTFcgTPDYIAPEIILYQ-----------------PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELF 556
Cdd:cd14171 159 AKVDQ-GDLMTPQF--TPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71986426 557 TA-----ITEHNVSYP----KSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd14171 236 TKdmkrkIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERM 278
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
354-552 8.19e-25

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: 104.46  E-value: 8.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSP--NCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMY-QIQQVGKFKEPVAVFYAAEIAVGLFFLH--SKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIF-----GDATTK 505
Cdd:cd13978  79 LKSlLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKsisanRRRGTE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEII---LYQPYGKSvDWWAYGVLLFEMLAGQPPFDGEDE 552
Cdd:cd13978 159 NLGGTPIYMAPEAFddfNKKPTSKS-DVYSFAIVIWAVLTRKEPFENAIN 207
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
348-611 8.62e-25

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 104.56  E-value: 8.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDDVECTMTEKRVLALPEKPSFLVaLHSCFQTMDRLYFVME 427
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVK----VKGADQVLVKKEISILNIARHRNILR-LHESFESHEELVMIFE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML--ERDGHIKITDFGMCKENIFGDATT 504
Cdd:cd14104  77 FISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctRRGSYIKIIEFGQSRQLKPGDKFR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCgTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCKA 580
Cdd:cd14104 157 LQYT-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDFVDR 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 71986426 581 LLIKNPSKRLgctgddesASRDIKEHPFFRR 611
Cdd:cd14104 236 LLVKERKSRM--------TAQEALNHPWLKQ 258
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
353-609 8.66e-25

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: 104.89  E-value: 8.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKvlkKdvIIQDDDV---ECTMTekRVLALPEkpsfLVALHSCFQTMDR------LY 423
Cdd:cd14137  11 VIGSGSFGVVYQAKLLETGEVVAIK---K--VLQDKRYknrELQIM--RRLKHPN----IVKLKYFFYSSGEkkdevyLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNggDLMYQ-IQQVGKFKEPVAVF----YAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERDGHIKITDFGMCKEN 497
Cdd:cd14137  80 LVMEYMP--ETLYRvIRHYSKNKQTIPIIyvklYSYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSAKRL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IFGDATTKTFCgTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI-------TEH-----NV 564
Cdd:cd14137 158 VPGEPNVSYIC-SRYYRAPELIFgATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIikvlgtpTREqikamNP 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986426 565 SY---------PKSLSK--------EAVSLCKALLIKNPSKRLgctgddeSASrDIKEHPFF 609
Cdd:cd14137 237 NYtefkfpqikPHPWEKvfpkrtppDAIDLLSKILVYNPSKRL-------TAL-EALAHPFF 290
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
351-561 1.18e-24

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 104.93  E-value: 1.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVectmTEKRVLAL-----PEKPSFLVALHSCFQTMDRLYFV 425
Cdd:cd14210  18 LSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQAL----VEVKILKHlndndPDDKHNIVRYKDSFIFRGHLCIV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVnGGDLmYQIQQVGKFKE---PVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML--ERDGHIKITDFGM-CKENif 499
Cdd:cd14210  94 FELL-SINL-YELLKSNNFQGlslSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFGSsCFEG-- 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986426 500 gdATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14210 170 --EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIME 229
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
354-547 1.38e-24

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 104.27  E-value: 1.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEC-------TMTEKRVLALPEKPSFLVALhscfQTMDRLYFVM 426
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCleiqimkRLNHPNVVAARDVPEGLQKL----APNDLPLLAM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDL---MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE----RDGHiKITDFGMCKENIF 499
Cdd:cd14038  78 EYCQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqgeqRLIH-KIIDLGYAKELDQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71986426 500 GDATTkTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd14038 157 GSLCT-SFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
104-156 1.42e-24

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 96.96  E-value: 1.42e-24
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCGTD 156
Cdd:cd20838   3 HRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNCGVN 55
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
353-547 1.46e-24

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 103.53  E-value: 1.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTtkELFAIKVLKKDviiQDDDVECTM----TEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEF 428
Cdd:cd14148   1 IIGVGGFGKVYKGLWRG--EEVAVKAARQD---PDEDIAVTAenvrQEARLFWMLQHPN-IIALRGVCLNPPHLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIqqVGKFKEP-VAVFYAAEIAVGLFFLHSKG---IIYRDLKLDNVM-LER-------DGHIKITDFGMCKE 496
Cdd:cd14148  75 ARGGALNRAL--AGKKVPPhVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILiLEPienddlsGKTLKITDFGLARE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 497 niFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd14148 153 --WHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
175-295 1.85e-24

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176022 [Multi-domain]  Cd Length: 116  Bit Score: 98.48  E-value: 1.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLIPEdsgcksKQKTKTLRATLNPQWNETFTYKLLPgDKDRRLSIEVWDWDRTS 254
Cdd:cd08376   2 VTIVLVEGKNLPPMDDNGLSDPYVKFRLGNE------KYKSKVCSKTLNPQWLEQFDLHLFD-DQSQILEIEVWDKDTGK 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71986426 255 RNDFMGSLSFGISEL-MKEAASGWYKLLSAEEGEFYNINITP 295
Cdd:cd08376  75 KDEFIGRCEIDLSALpREQTHSLELELEDGEGSLLLLLTLTG 116
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
353-609 4.97e-24

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: 101.96  E-value: 4.97e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLK--KDVIIQdddvecTMTEKRVLAL-----PEKPSFLVALHSCFQTMDRLYFV 425
Cdd:cd14133   6 VLGKGTFGQVVKCYDLLTGEEVALKIIKnnKDYLDQ------SLDEIRLLELlnkkdKADKYHIVRLKDVFYFKNHLCIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVngGDLMYQIQQVGKFKE---PVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE--RDGHIKITDFGMCkenifg 500
Cdd:cd14133  80 FELL--SQNLYEFLKQNKFQYlslPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLAsySRCQIKIIDFGSS------ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 dattktfCGTPD----------YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSL 570
Cdd:cd14133 152 -------CFLTQrlysyiqsryYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHM 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71986426 571 SKEA-------VSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14133 225 LDQGkaddelfVDFLKKLLEIDPKERP--------TASQALSHPWL 262
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
169-269 5.37e-24

C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176000 [Multi-domain]  Cd Length: 123  Bit Score: 97.35  E-value: 5.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 169 HIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGcKSKQKTKTLRATLNPQWNETFTYKLLPGDKDRR--LSIE 246
Cdd:cd04035  11 DPANSALHCTIIRAKGLKAMDANGLSDPYVKLNLLPGASK-ATKLRTKTVHKTRNPEFNETLTYYGITEEDIQRktLRLL 89
                        90       100
                ....*....|....*....|...
gi 71986426 247 VWDWDRTsRNDFMGSLSFGISEL 269
Cdd:cd04035  90 VLDEDRF-GNDFLGETRIPLKKL 111
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
104-153 7.49e-24

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 94.43  E-value: 7.49e-24
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20837   1 HRFKVYNYMSPTFCDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
354-590 9.79e-24

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: 102.79  E-value: 9.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtmtekrVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14176  27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI------LLRYGQHPN-IITLKDVYDDGKYVYVVTELMKGGE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQI--QQVGKFKEPVAVFYAaeIAVGLFFLHSKGIIYRDLKLDNVM-LERDGH---IKITDFGMCKENIFGDATTKTF 507
Cdd:cd14176 100 LLDKIlrQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTP 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED---ELFTAITEHNVS----YPKSLSKEAVSLCKA 580
Cdd:cd14176 178 CYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDtpeEILARIGSGKFSlsggYWNSVSDTAKDLVSK 257
                       250
                ....*....|
gi 71986426 581 LLIKNPSKRL 590
Cdd:cd14176 258 MLHVDPHQRL 267
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
354-609 1.17e-23

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 100.73  E-value: 1.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVL-----KKDVIIQDDDVECTMTEKRVLALPEKpsflvalhscFQTMDRLYFVMEF 428
Cdd:cd14107  10 IGRGTFGFVKRVTHKGNGECCAAKFIplrssTRARAFQERDILARLSHRRLTCLLDQ----------FETRKTLILILEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---ERDgHIKITDFGMCKENIFGDATTK 505
Cdd:cd14107  80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvspTRE-DIKICDFGFAQEITPSEHQFS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFcGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK----SLSKEAVSLCKAL 581
Cdd:cd14107 159 KY-GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTpeitHLSEDAKDFIKRV 237
                       250       260
                ....*....|....*....|....*...
gi 71986426 582 LIKNPSKRlgctgddESASrDIKEHPFF 609
Cdd:cd14107 238 LQPDPEKR-------PSAS-ECLSHEWF 257
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
359-590 1.60e-23

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 100.48  E-value: 1.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 359 FGKVLLGEQKTTKELFAIK-VLKKDviiQDDDVECTMTEKRVLALPEKPSFLvALHSCFQTMDRLYFVMEFVNGGDLMYQ 437
Cdd:cd14088  14 FCEIFRAKDKTTGKLYTCKkFLKRD---GRKVRKAAKNEINILKMVKHPNIL-QLVDVFETRKEYFIFLELATGREVFDW 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 438 IQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE---RDGHIKITDFGMCK-ENifgdATTKTFCGTPDY 513
Cdd:cd14088  90 ILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKlEN----GLIKEPCGTPEY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 514 IAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDE--------LFTAIT----EHNVSYPKSLSKEAVSLCKAL 581
Cdd:cd14088 166 LAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDdyenhdknLFRKILagdyEFDSPYWDDISQAAKDLVTRL 245

                ....*....
gi 71986426 582 LIKNPSKRL 590
Cdd:cd14088 246 MEVEQDQRI 254
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
353-584 2.22e-23

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: 100.12  E-value: 2.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqdddvECTMTEKRVLALPEKPSFL--------VALHSCFQ-TMDR-L 422
Cdd:cd06652   9 LLGQGAFGRVYLCYDADTGRELAVKQVQFDP-------ESPETSKEVNALECEIQLLknllheriVQYYGCLRdPQERtL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFG 500
Cdd:cd06652  82 SIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlQTICL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DAT-TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITE-HNVSYPKSLSKEAVSL 577
Cdd:cd06652 162 SGTgMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWaEFEAMAAIFKIATQpTNPQLPAHVSDHCRDF 241

                ....*..
gi 71986426 578 CKALLIK 584
Cdd:cd06652 242 LKRIFVE 248
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
354-590 2.44e-23

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: 100.86  E-value: 2.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECtmtekrVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14178  11 IGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEI------LLRYGQHPN-IITLKDVYDDGKFVYLVMELMRGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM-LERDGH---IKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd14178  84 LLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDE--DELFTAITEHNVSYP----KSLSKEAVSLCKALL 582
Cdd:cd14178 164 TANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFaNGPDDtpEEILARIGSGKYALSggnwDSISDAAKDIVSKML 243

                ....*...
gi 71986426 583 IKNPSKRL 590
Cdd:cd14178 244 HVDPHQRL 251
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
354-609 2.52e-23

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: 100.44  E-value: 2.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAikvLKKDVIIQDDD-VECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGg 432
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVA---LKKIRLETEDEgVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLDL- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVF--YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGdATTKTFCG- 509
Cdd:cd07835  83 DLKKYMDSSPLTGLDPPLIksYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLAR--AFG-VPVRTYTHe 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 --TPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELF-----------------TAITEHNVSYPK 568
Cdd:cd07835 160 vvTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEiDQLFrifrtlgtpdedvwpgvTSLPDYKPTFPK 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 569 -----------SLSKEAVSLCKALLIKNPSKRLgctgddeSAsRDIKEHPFF 609
Cdd:cd07835 240 warqdlskvvpSLDEDGLDLLSQMLVYDPAKRI-------SA-KAALQHPYF 283
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
345-589 2.75e-23

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: 100.14  E-value: 2.75e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDDVEctmtEKRVLALPEKPSFL-----VALHSCFQTM 419
Cdd:cd14046   5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK----LRSESKN----NSRILREVMLLSRLnhqhvVRYYQAWIER 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 DRLYFVMEFVNGGDLMYQIQQvGKFKEPVAVF-YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI 498
Cdd:cd14046  77 ANLYIQMEYCEKSTLRDLIDS-GLFQDTDRLWrLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 F--------------------GDATTKTfcGTPDYIAPEII--LYQPYGKSVDWWAYGVLLFEMLagQPPFDGEDEDELF 556
Cdd:cd14046 156 LnvelatqdinkstsaalgssGDLTGNV--GTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMC--YPFSTGMERVQIL 231
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71986426 557 TAITEHNVSYP----KSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd14046 232 TALRSVSIEFPpdfdDNKHSKQAKLIRWLLNHDPAKR 268
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
348-610 3.43e-23

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: 100.34  E-value: 3.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDD-VECTmtekrvlALPE-------KPSFLVALHSCFQTM 419
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDgINFT-------ALREikllqelKHPNIIGLLDVFGHK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 DRLYFVMEFVnGGDLmyqiQQVgkFKEPVAVFYAAEIAV-------GLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG 492
Cdd:cd07841  75 SNINLVFEFM-ETDL----EKV--IKDKSIVLTPADIKSymlmtlrGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 493 MCKenIFGDA----TTKTFcgTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DEL---FTAI---T 560
Cdd:cd07841 148 LAR--SFGSPnrkmTHQVV--TRWYRAPELLFgARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDiDQLgkiFEALgtpT 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426 561 EHN-------------VSYPK--------SLSKEAVSLCKALLIKNPSKRLGCtgddesasRDIKEHPFFR 610
Cdd:cd07841 224 EENwpgvtslpdyvefKPFPPtplkqifpAASDDALDLLQRLLTLNPNKRITA--------RQALEHPYFS 286
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
433-590 3.78e-23

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 100.17  E-value: 3.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKF--KEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH-IKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd13974 118 NLQHYVIREKRLseREALVIFY--DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQRG 195
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS--LSKEAVSLCKALLIKNP 586
Cdd:cd13974 196 SPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDgrVSENTVCLIRKLLVLNP 275

                ....
gi 71986426 587 SKRL 590
Cdd:cd13974 276 QKRL 279
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
423-589 8.00e-23

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 102.95  E-value: 8.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGmckenI---F 499
Cdd:NF033483  83 YIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFG-----IaraL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  500 GDAT---TKTFCGTPDYIAPEiilyQPYGKSV----DWWAYGVLLFEMLAGQPPFDGED----------EDelFTAITEH 562
Cdd:NF033483 158 SSTTmtqTNSVLGTVHYLSPE----QARGGTVdarsDIYSLGIVLYEMLTGRPPFDGDSpvsvaykhvqED--PPPPSEL 231
                        170       180
                 ....*....|....*....|....*..
gi 71986426  563 NVSYPKSLskEAVSLcKAlLIKNPSKR 589
Cdd:NF033483 232 NPGIPQSL--DAVVL-KA-TAKDPDDR 254
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
352-589 9.42e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 98.00  E-value: 9.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQ----DDDVECTMT---EKRVLALPEKPSfLVALHSCFQTMDRLYF 424
Cdd:cd14101   6 NLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklPGVNPVPNEvalLQSVGGGPGHRG-VIRLLDWFEIPEGFLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEF-VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDGHIKITDFG---MCKENIF 499
Cdd:cd14101  85 VLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGsgaTLKDSMY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDattktFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDgEDEDelftaITEHNVSYPKSLSKEAVSLC 578
Cdd:cd14101 165 TD-----FDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFE-RDTD-----ILKAKPSFNKRVSNDCRSLI 233
                       250
                ....*....|.
gi 71986426 579 KALLIKNPSKR 589
Cdd:cd14101 234 RSCLAYNPSDR 244
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
351-622 1.03e-22

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: 98.65  E-value: 1.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSFLVALHSCF----QTMdrLYFVM 426
Cdd:cd06621   6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTD---PNPDVQKQILRELEINKSCASPYIVKYYGAFldeqDSS--IGIAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDL--MYQ--IQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGDA 502
Cdd:cd06621  81 EYCEGGSLdsIYKkvKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGE--LVNS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED-----ELFTAITehNVSYPK--------- 568
Cdd:cd06621 159 LAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpiELLSYIV--NMPNPElkdepengi 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 569 SLSKEAVSLCKALLIKNPSKRLGctgddesaSRDIKEHPffrridWFKIETRQI 622
Cdd:cd06621 237 KWSESFKDFIEKCLEKDGTRRPG--------PWQMLAHP------WIKAQEKKK 276
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
352-610 1.24e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 98.27  E-value: 1.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLK---KDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEF 428
Cdd:cd06630   6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSfcrNSSSEQEEVVEAIREEIRMMARLNHPN-IVRMLGATQHKSHFNIFVEW 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG-HIKITDFG----MCKENIFGDAT 503
Cdd:cd06630  85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGaaarLASKGTGAGEF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI-----TEHNVSYPKSLSKEAVSLC 578
Cdd:cd06630 165 QGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkiasATTPPPIPEHLSPGLRDVT 244
                       250       260       270
                ....*....|....*....|....*....|..
gi 71986426 579 KALLIKNPSKRlgctgddeSASRDIKEHPFFR 610
Cdd:cd06630 245 LRCLELQPEDR--------PPARELLKHPVFT 268
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
354-547 1.29e-22

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 98.67  E-value: 1.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVAL----HSCFQTMDRLYFV-MEF 428
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARdvppELEKLSPNDLPLLaMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGK---FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGMCKENIFGDA 502
Cdd:cd13989  81 CSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKELDQGSL 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 71986426 503 TTkTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd13989 161 CT-SFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
350-589 1.55e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 97.50  E-value: 1.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLGEQKTTKELFAIKV--LKKDVIIQDDDVectMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd08221   4 PVRVLGRGAFGEAVLYRKTEDNSLVVWKEvnLSRLSEKERRDA---LNEIDILSLLNHDN-IITYYNHFLDGESLFIEME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQI-QQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTK 505
Cdd:cd08221  80 YCNGGNLHDKIaQQKNQlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS-LSKEAVSLCKALLIK 584
Cdd:cd08221 160 SIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEqYSEEIIQLVHDCLHQ 239

                ....*
gi 71986426 585 NPSKR 589
Cdd:cd08221 240 DPEDR 244
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
348-609 1.85e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 97.96  E-value: 1.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVME 427
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT--ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGgDL--MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGdATTK 505
Cdd:cd07860  80 FLHQ-DLkkFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARA--FG-VPVR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 TFCG---TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELF-----------------TAITEHN 563
Cdd:cd07860 156 TYTHevvTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEiDQLFrifrtlgtpdevvwpgvTSMPDYK 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 564 VSYPK-----------SLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd07860 236 PSFPKwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRI--------SAKAALAHPFF 284
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
348-610 1.92e-22

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 99.29  E-value: 1.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKK---DVIiqddDVECTMTEKRVLALPEKPSFLVALH-----SCFQTM 419
Cdd:cd07851  17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfqSAI----HAKRTYRELRLLKHMKHENVIGLLDvftpaSSLEDF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 DRLYFVMEFVnGGDLmYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENif 499
Cdd:cd07851  93 QDVYLVTHLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHT-- 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 gDATTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED---------------EDELFTAIT-EH 562
Cdd:cd07851 169 -DDEMTGYVATRWYRAPEIMLnWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDhidqlkrimnlvgtpDEELLKKISsES 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986426 563 NVSYPKSL---------------SKEAVSLCKALLIKNPSKRLgctgddeSASRDIkEHPFFR 610
Cdd:cd07851 248 ARNYIQSLpqmpkkdfkevfsgaNPLAIDLLEKMLVLDPDKRI-------TAAEAL-AHPYLA 302
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
354-555 2.07e-22

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 97.18  E-value: 2.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDviiqdDDVECTMTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVNGGD 433
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRF-----DEQRSFLKEVKLMRRLSHPNILRFIGVCVKD-NKLNFITEYVNGGT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIK---ITDFGMCKEniFGDATTK---- 505
Cdd:cd14065  75 LEELLKSMDEqLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLARE--MPDEKTKkpdr 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 506 ----TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPfdgeDEDEL 555
Cdd:cd14065 153 kkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVPA----DPDYL 202
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
354-609 2.49e-22

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: 97.63  E-value: 2.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFA--------------------IKVLKK---DVIIQdddVECTMTEKrvLALPEKPS-FL 409
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVAlkkirmenekegfpitaireIKLLQKldhPNVVR---LKEIVTSK--GSAKYKGSiYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 410 ValhscFQTMDRlyfvmefvnggDLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI 488
Cdd:cd07840  82 V-----FEYMDH-----------DLTGLLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 489 TDFGMckenifgdATTKTFCGTPDYI---------APEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTA 558
Cdd:cd07840 146 ADFGL--------ARPYTKENNADYTnrvitlwyrPPELLLGATrYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEK 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 559 ITE-----------------------HNVSYPKSL--------SKEAVSLCKALLIKNPSKRLgctgddeSAsRDIKEHP 607
Cdd:cd07840 218 IFElcgspteenwpgvsdlpwfenlkPKKPYKRRLrevfknviDPSALDLLDKLLTLDPKKRI-------SA-DQALQHE 289

                ..
gi 71986426 608 FF 609
Cdd:cd07840 290 YF 291
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
175-287 2.55e-22

C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176005 [Multi-domain]  Cd Length: 115  Bit Score: 92.25  E-value: 2.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLipeDSgcKSKQKTKTLRATLNPQWNETFTYKlLPGDKDRRLSIEVWDWDRTS 254
Cdd:cd04040   1 LTVDVISAENLPSADRNGKSDPFVKFYL---NG--EKVFKTKTIKKTLNPVWNESFEVP-VPSRVRAVLKVEVYDWDRGG 74
                        90       100       110
                ....*....|....*....|....*....|...
gi 71986426 255 RNDFMGSLSFGISELMKEAASGWYKLLSAEEGE 287
Cdd:cd04040  75 KDDLLGSAYIDLSDLEPEETTELTLPLDGQGGG 107
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
345-610 2.90e-22

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 97.87  E-value: 2.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTM----- 419
Cdd:cd06637   5 AGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKnppgm 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 -DRLYFVMEFVNGGDLMYQIQQV--GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd06637  81 dDQLWLVMEFCGAGSVTDLIKNTkgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTFCGTPDYIAPEIILYQ-----PYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFtaITEHNVS---YP 567
Cdd:cd06637 161 LDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLcDMHPMRALF--LIPRNPAprlKS 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71986426 568 KSLSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFFR 610
Cdd:cd06637 239 KKWSKKFQSFIESCLVKNHSQR--------PSTEQLMKHPFIR 273
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
353-549 3.42e-22

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 96.23  E-value: 3.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTtKELFAIKVLKKDvIIQDDDVEcTMTEKRVLALPEKPSFLVALHSCFQTMDrLYFVMEFVNGG 432
Cdd:cd05085   3 LLGKGNFGEVYKGTLKD-KTPVAVKTCKED-LPQELKIK-FLSEARILKQYDHPNIVKLIGVCTQRQP-IYIVMELVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 D-LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05085  79 DfLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQIP 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 71986426 512 -DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05085 159 iKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPG 198
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
348-610 3.59e-22

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: 97.37  E-value: 3.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKdviIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDR-----L 422
Cdd:cd06639  24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDP---ISDVDEEIEAEYNILRSLPNHPN-VVKFYGMFYKADQyvggqL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGG---DLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI 498
Cdd:cd06639 100 WLVLELCNGGsvtELVKGLLKCGqRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 FGDATTKTFCGTPDYIAPEIILYQ-----PYGKSVDWWAYGVLLFEMLAGQPP-FDGEDEDELFTaITEH---NVSYPKS 569
Cdd:cd06639 180 SARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPlFDMHPVKALFK-IPRNpppTLLNPEK 258
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71986426 570 LSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFFR 610
Cdd:cd06639 259 WCRGFSHFISQCLIKDFEKRPSVT--------HLLEHPFIK 291
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
353-589 3.69e-22

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: 96.63  E-value: 3.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLkkdvIIQD-DDVECTMTEKRVLALPEKPSFLVALHSC--FQTMDRLYF--VME 427
Cdd:cd13985   7 QLGEGGFSYVYLAHDVNTGRRYALKRM----YFNDeEQLRVAIKEIEIMKRLCGHPNIVQYYDSaiLSSEGRKEVllLME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVnGGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKG--IIYRDLKLDNVMLERDGHIKITDFG----------- 492
Cdd:cd13985  83 YC-PGSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattehypler 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 493 -----MCKENIfgDATTktfcgTPDYIAPEII---LYQPYGKSVDWWAYGVLLFEMLAGQPPFDgedeDELFTAITEHNV 564
Cdd:cd13985 162 aeevnIIEEEI--QKNT-----TPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFD----ESSKLAIVAGKY 230
                       250       260
                ....*....|....*....|....*..
gi 71986426 565 SYPK--SLSKEAVSLCKALLIKNPSKR 589
Cdd:cd13985 231 SIPEqpRYSPELHDLIRHMLTPDPAER 257
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
354-547 4.44e-22

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 96.91  E-value: 4.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTE----------KRVLALPEKPSFLVAlhscfqtmDRLY 423
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQimkklnhpnvVKACDVPEEMNFLVN--------DVPL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDL---MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-ERDGHI--KITDFGMCKEN 497
Cdd:cd14039  73 LAMEYCSGGDLrklLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDL 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IFGDATTkTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd14039 153 DQGSLCT-SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
351-609 4.84e-22

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: 96.72  E-value: 4.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDV--ECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEF 428
Cdd:cd07846   6 LGLVGEGSYGMVMKCRHKETGQIVAIKKFLES---EDDKMvkKIAMREIKMLKQLRHEN-LVNLIEVFRRKKRWYLVFEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE-NIFGDATTKtF 507
Cdd:cd07846  82 VDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlAAPGEVYTD-Y 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGE-DEDELF-------TAITEHNV-------------- 564
Cdd:cd07846 161 VATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDsDIDQLYhiikclgNLIPRHQElfqknplfagvrlp 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 565 ----------SYPKsLSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFF 609
Cdd:cd07846 241 evkeveplerRYPK-LSGVVIDLAKKCLHIDPDKRPSCS--------ELLHHEFF 286
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
347-547 5.54e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 96.49  E-value: 5.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDdvECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFVM 426
Cdd:cd06619   2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQ--KQIMSELEILYKCDSP-YIIGFYGAFFVENRISICT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDL-MYqiqqvGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIfgDATTK 505
Cdd:cd06619  79 EFMDGGSLdVY-----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--NSIAK 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71986426 506 TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd06619 152 TYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPY 193
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
343-589 6.59e-22

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: 95.59  E-value: 6.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVEctmtEKRVLALPEKPSfLVALHSCFQTMDRL 422
Cdd:cd05059   1 IDPSELTFLKELGSGQFGVVHLGKWRGKIDV-AIKMIKEGSMSEDDFIE----EAKVMMKLSHPK-LVQLYGVCTKQRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEF-VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeNIFGD 501
Cdd:cd05059  75 FIVTEYmANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLAR-YVLDD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTFcGTP---DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITEHNVSY-PKSLSKEAVS 576
Cdd:cd05059 154 EYTSSV-GTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGYRLYrPHLAPTEVYT 232
                       250
                ....*....|...
gi 71986426 577 LCKALLIKNPSKR 589
Cdd:cd05059 233 IMYSCWHEKPEER 245
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
160-260 9.04e-22

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 91.17  E-value: 9.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 160 KRGRLR--IEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDsgcKSKQKTKTLRATLNPQWNETFTYKLLPG 237
Cdd:cd08385   1 KLGKLQfsLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLPDK---KKKFETKVHRKTLNPVFNETFTFKVPYS 77
                        90       100
                ....*....|....*....|....
gi 71986426 238 D-KDRRLSIEVWDWDRTSRNDFMG 260
Cdd:cd08385  78 ElGNKTLVFSVYDFDRFSKHDLIG 101
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
353-593 9.32e-22

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 96.26  E-value: 9.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKkDVIIQDDDVEctmTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14170   9 VLGLGINGKVLQIFNKRTQEKFALKMLQ-DCPKARREVE---LHWRASQCPHIVRIVDVYENLYAGRKCLLIVMECLDGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER---DGHIKITDFGMCKENIFGDATTkTF 507
Cdd:cd14170  85 ELFSRIQDRGDqaFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLT-TP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH----NVSYPKS----LSKEAVSLCK 579
Cdd:cd14170 164 CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRirmgQYEFPNPewseVSEEVKMLIR 243
                       250
                ....*....|....
gi 71986426 580 ALLIKNPSKRLGCT 593
Cdd:cd14170 244 NLLKTEPTQRMTIT 257
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
354-547 1.12e-21

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: 95.85  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKdviIQDDDVECTMTEKRVLALPEKPSfLVALHSCF-----QTMDRLYFVMEF 428
Cdd:cd06638  26 IGKGTYGKVFKVLNKKNGSKAAVKILDP---IHDIDEEIEAEYNILKALSDHPN-VVKFYGMYykkdvKNGDQLWLVLEL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGG---DLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATT 504
Cdd:cd06638 102 CNGGsvtDLVKGFLKRGeRMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71986426 505 KTFCGTPDYIAPEII-----LYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd06638 182 NTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPL 229
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
175-281 1.13e-21

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 91.01  E-value: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKlipedsgCKSK-QKTKTLRATLNPQWNETFTYKLLPGdKDRRLSIEVWDWDRT 253
Cdd:cd04025   2 LRCHVLEARDLAPKDRNGTSDPFVRVF-------YNGQtLETSVVKKSCYPRWNEVFEFELMEG-ADSPLSVEVWDWDLV 73
                        90       100
                ....*....|....*....|....*....
gi 71986426 254 SRNDFMGSLSFGISELMKE-AASGWYKLL 281
Cdd:cd04025  74 SKNDFLGKVVFSIQTLQQAkQEEGWFRLL 102
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
347-589 1.17e-21

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 95.03  E-value: 1.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLK-KDVIIQDDDVECtMTEKRVLALPEKPSFLVALHScFQTMDRLYFV 425
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQiFEMMDAKARQDC-LKEIDLLQQLNHPNIIKYLAS-FIENNELNIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGD 501
Cdd:cd08224  79 LELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR--FFSS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTF--CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED--ELFTAITehNVSYP----KSLSKE 573
Cdd:cd08224 157 KTTAAHslVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIE--KCEYPplpaDLYSQE 234
                       250
                ....*....|....*.
gi 71986426 574 AVSLCKALLIKNPSKR 589
Cdd:cd08224 235 LRDLVAACIQPDPEKR 250
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
348-609 1.66e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 96.06  E-value: 1.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKdviIQDDDVECtmteKRVLAlpEkpsflVALHSCFQ---------- 417
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISN---VFDDLIDA----KRILR--E-----IKILRHLKheniiglldi 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 -------TMDRLYFVMEFVnGGDLmyqiQQVGKFKEPVAV----FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI 486
Cdd:cd07834  68 lrppspeEFNDVYIVTELM-ETDL----HKVIKSPQPLTDdhiqYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 487 KITDFGMCKE-NIFGDATTKTfcgtpDYI------APEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED------- 551
Cdd:cd07834 143 KICDFGLARGvDPDEDKGFLT-----EYVvtrwyrAPELLLsSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDyidqlnl 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 552 ---------EDELFTAITEHNVSYPKSLSK---------------EAVSLCKALLIKNPSKRLgcTGDDesASRdikeHP 607
Cdd:cd07834 218 ivevlgtpsEEDLKFISSEKARNYLKSLPKkpkkplsevfpgaspEAIDLLEKMLVFNPKKRI--TADE--ALA----HP 289

                ..
gi 71986426 608 FF 609
Cdd:cd07834 290 YL 291
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
343-575 1.92e-21

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: 94.54  E-value: 1.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVEctmtEKRVLALPEKPSfLVALHSCFQTMDRL 422
Cdd:cd05114   1 INPSELTFMKELGSGLFGVVRLGKWRAQYKV-AIKAIREGAMSEEDFIE----EAKVMMKLTHPK-LVQLYGVCTQQKPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGD 501
Cdd:cd05114  75 YIVTEFMENGCLLnYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQ 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 502 ATTKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITEHNVSYPKSLSKEAV 575
Cdd:cd05114 155 YTSSSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSV 230
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
347-589 1.96e-21

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 94.48  E-value: 1.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDDVEctmTEKRVLALPEKPSfLVALHSCFQTMDR----- 421
Cdd:cd14047   7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK----LNNEKAE---REVKALAKLDHPN-IVRYNGCWDGFDYdpets 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 -----------LYFVMEFVNGGDLMYQIQQVGKFK----EPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI 486
Cdd:cd14047  79 ssnssrsktkcLFIQMEFCEKGTLESWIEKRNGEKldkvLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGKV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 487 KITDFGMCKENIFGDATTKTFcGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPpfDGEDEDELFTAITEHNVS- 565
Cdd:cd14047 157 KIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCD--SAFEKSKFWTDLRNGILPd 233
                       250       260
                ....*....|....*....|....*
gi 71986426 566 -YPKSLSKEaVSLCKALLIKNPSKR 589
Cdd:cd14047 234 iFDKRYKIE-KTIIKKMLSKKPEDR 257
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
354-589 2.03e-21

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: 95.08  E-value: 2.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTekrvlaLPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14177  12 IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMR------YGQHPN-IITLKDVYDDGRYVYLVTELMKGGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQI--QQVGKFKEPVAVFYAaeIAVGLFFLHSKGIIYRDLKLDNVMLERDG----HIKITDFGMCKENIFGDATTKTF 507
Cdd:cd14177  85 LLDRIlrQKFFSEREASAVLYT--ITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGENGLLLTP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDE--DELFTAITEHNVSYP----KSLSKEAVSLCKA 580
Cdd:cd14177 163 CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFaNGPNDtpEEILLRIGSGKFSLSggnwDTVSDAAKDLLSH 242

                ....*....
gi 71986426 581 LLIKNPSKR 589
Cdd:cd14177 243 MLHVDPHQR 251
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
345-608 2.96e-21

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: 94.30  E-value: 2.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTM----- 419
Cdd:cd06636  15 AGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKsppgh 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 -DRLYFVMEFVNGGDLMYQIQQV--GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd06636  91 dDQLWLVMEFCGAGSVTDLVKNTkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTFCGTPDYIAPEIILYQ-----PYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFtaITEHNVS---YP 567
Cdd:cd06636 171 LDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRALF--LIPRNPPpklKS 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71986426 568 KSLSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPF 608
Cdd:cd06636 249 KKWSKKFIDFIEGCLVKNYLSR--------PSTEQLLKHPF 281
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
171-269 4.41e-21

C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176032 [Multi-domain]  Cd Length: 125  Bit Score: 89.31  E-value: 4.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 171 ENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDsgcKSKQKTKTLRATLNPQWNETFTYKLLPGDK--DRRLSIEVW 248
Cdd:cd08386  14 QESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDK---KHKLETKVKRKNLNPHWNETFLFEGFPYEKlqQRVLYLQVL 90
                        90       100
                ....*....|....*....|.
gi 71986426 249 DWDRTSRNDFMGSLSFGISEL 269
Cdd:cd08386  91 DYDRFSRNDPIGEVSLPLNKV 111
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
174-265 5.22e-21

C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 89.38  E-value: 5.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKsKQKTKTLRATLNPQWNETFTYKLLPGD-KDRRLSIEVWDWDR 252
Cdd:cd08402  16 KLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLK-KKKTTIKKRTLNPYYNESFSFEVPFEQiQKVHLIVTVLDYDR 94
                        90
                ....*....|...
gi 71986426 253 TSRNDFMGSLSFG 265
Cdd:cd08402  95 IGKNDPIGKVVLG 107
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
39-91 5.63e-21

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 86.34  E-value: 5.63e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71986426    39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGA 91
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
343-575 6.81e-21

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 92.64  E-value: 6.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVEctmtEKRVLALPEKPSfLVALHSCFQTMDRL 422
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYDV-AIKMIKEGSMSEDEFIE----EAKVMMNLSHEK-LVQLYGVCTKQRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVF-YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGD 501
Cdd:cd05113  75 FIITEYMANGCLLNYLREMRKRFQTQQLLeMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 502 ATTKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITEHNVSYPKSLSKEAV 575
Cdd:cd05113 155 YTSSVGSKFPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGLRLYRPHLASEKV 230
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
347-539 7.44e-21

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: 93.26  E-value: 7.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVL-LGEQKTTKELFAIKVLKKDVIiQDDDVECTMTEKRVL-ALPEKPS-FLVALHSCFQTMDRLY 423
Cdd:cd14052   1 RFANVELIGSGEFSQVYkVSERVPTGKVYAVKKLKPNYA-GAKDRLRRLEEVSILrELTLDGHdNIVQLIDSWEYHGHLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFK--EPVAVFYA-AEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCkeNIFG 500
Cdd:cd14052  80 IQTELCENGSLDVFLSELGLLGrlDEFRVWKIlVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA--TVWP 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 71986426 501 DATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFE 539
Cdd:cd14052 158 LIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
347-609 7.77e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 93.25  E-value: 7.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLES--EEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGgDLMYQIQQV--GKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFG--- 500
Cdd:cd07861  79 EFLSM-DLKKYLDSLpkGKYMDAELVkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARA--FGipv 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATTKTFCgTPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELF-----------------TAITE 561
Cdd:cd07861 156 RVYTHEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEiDQLFrifrilgtptediwpgvTSLPD 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 562 HNVSYPK-----------SLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd07861 235 YKNTFPKwkkgslrtavkNLDEDGLDLLEKMLIYDPAKRI--------SAKKALVHPYF 285
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
352-589 8.26e-21

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 92.33  E-value: 8.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSF---LVALHSCFQTMDRLYFVMEF 428
Cdd:cd14102   6 SVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVGSGfrgVIKLLDWYERPDGFLIVMER 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VN-GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDGHIKITDFG---MCKENIFGDat 503
Cdd:cd14102  86 PEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGsgaLLKDTVYTD-- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 tktFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEdelftaITEHNVSYPKSLSKEAVSLCKALL 582
Cdd:cd14102 164 ---FDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEE------ILRGRLYFRRRVSPECQQLIKWCL 234

                ....*..
gi 71986426 583 IKNPSKR 589
Cdd:cd14102 235 SLRPSDR 241
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
353-584 8.85e-21

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: 92.84  E-value: 8.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPE-KPSFLVALHSCFQtmDR----LYFVME 427
Cdd:cd06651  14 LLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNlQHERIVQYYGCLR--DRaektLTIFME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFGDAT-T 504
Cdd:cd06651  92 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTICMSGTgI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITE-HNVSYPKSLSKEAVSLCKALL 582
Cdd:cd06651 172 RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWaEYEAMAAIFKIATQpTNPQLPSHISEHARDFLGCIF 251

                ..
gi 71986426 583 IK 584
Cdd:cd06651 252 VE 253
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
354-609 9.66e-21

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: 92.72  E-value: 9.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqdDDVECTMTEKRVLA---LPEKPsFLVALHSCF--QTMDRLYFVMEF 428
Cdd:cd07831   7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHF----KSLEQVNNLREIQAlrrLSPHP-NILRLIEVLfdRKTGRLALVFEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGdlMYQ-IQ-QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLeRDGHIKITDFGMCKeNIFGDATTKT 506
Cdd:cd07831  82 MDMN--LYElIKgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCR-GIYSKPPYTE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 FCGTPDYIAPEIIL---YqpYGKSVDWWAYGVLLFEMLAGQPPFDGEDE------------------DELFTAITEHNVS 565
Cdd:cd07831 158 YISTRWYRAPECLLtdgY--YGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiakihdvlgtpdaevLKKFRKSRHMNYN 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 566 YPK-----------SLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd07831 236 FPSkkgtglrkllpNASAEGLDLLKKLLAYDPDERI--------TAKQALRHPYF 282
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
160-270 1.29e-20

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 88.06  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 160 KRGRLRIEAHIEN--DQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPED--SGCKsKQKTKTLRATLNPQWNETFTYKLL 235
Cdd:cd04009   1 PYGVLTVKAYYRAseQSLRVEILNARNLLPLDSNGSSDPFVKVELLPRHlfPDVP-TPKTQVKKKTLFPLFDESFEFNVP 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71986426 236 PGDKDRR---LSIEVWDWDRTSRNDFMGSLSFGISELM 270
Cdd:cd04009  80 PEQCSVEgalLLFTVKDYDLLGSNDFEGEAFLPLNDIP 117
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
354-549 1.53e-20

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 91.74  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqDDDVECTMTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVNGGD 433
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLP--PDLKRKFLQEARILKQYDHPNIVKLIGVCVQK-QPIMIVMELVPGGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTfcGTPD 512
Cdd:cd05041  80 LLtFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSD--GLKQ 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71986426 513 ----YIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05041 158 ipikWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPG 199
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
346-607 1.83e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 92.82  E-value: 1.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiQDDDVECT-MTEKRVLALPEKPSfLVALHSCF--QTMDRL 422
Cdd:cd07845   7 TEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISsLREITLLLNLRHPN-IVELKEVVvgKHLDSI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNG--GDLMYQIQQvgKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENI 498
Cdd:cd07845  84 FLVMEYCEQdlASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARtyGLP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 FGDATTKTFcgTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE---------------- 561
Cdd:cd07845 162 AKPMTPKVV--TLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQllgtpnesiwpgfsdl 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 562 ---HNVSYPKS-----------LSKEAVSLCKALLIKNPSKRLgcTGDDESASRDIKEHP 607
Cdd:cd07845 240 plvGKFTLPKQpynnlkhkfpwLSEAGLRLLNFLLMYDPKKRA--TAEEALESSYFKEKP 297
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
172-266 1.91e-20

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 87.86  E-value: 1.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 172 NDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKsKQKTKTLRATLNPQWNETFTYKlLPGDKDRRLSIE--VWD 249
Cdd:cd08405  14 ANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRVE-KKKTVIKKRTLNPVFNESFIFN-IPLERLRETTLIitVMD 91
                        90
                ....*....|....*..
gi 71986426 250 WDRTSRNDFMGSLSFGI 266
Cdd:cd08405  92 KDRLSRNDLIGKIYLGW 108
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
344-609 4.71e-20

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: 91.61  E-value: 4.71e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 344 KASDFNFLTVLGKGSFGKVLLGEQKTTKELFAikvLKKdvIIQDDDVE----CTMTEKRVLALPEKPSFL-----VALHS 414
Cdd:cd07866   6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVA---LKK--ILMHNEKDgfpiTALREIKILKKLKHPNVVplidmAVERP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 415 CFQTMDRLYFVM-EFVNGGDL--MYQIQQVgKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDF 491
Cdd:cd07866  81 DKSKRKRGSVYMvTPYMDHDLsgLLENPSV-KLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 492 GMCKeNIFGDATTKTFCGTPD------------YIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGE-DEDEL-- 555
Cdd:cd07866 160 GLAR-PYDGPPPNPKGGGGGGtrkytnlvvtrwYRPPELLLgERRYTTAVDIWGIGCVFAEMFTRRPILQGKsDIDQLhl 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 556 -FTAI---TEHNVS----------------YPKSLS-------KEAVSLCKALLIKNPSKRLgctgddeSASrDIKEHPF 608
Cdd:cd07866 239 iFKLCgtpTEETWPgwrslpgcegvhsftnYPRTLEerfgklgPEGLDLLSKLLSLDPYKRL-------TAS-DALEHPY 310

                .
gi 71986426 609 F 609
Cdd:cd07866 311 F 311
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
343-589 5.27e-20

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: 90.96  E-value: 5.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL----KKDVIIQdddvecTMTEKRVLALPEKPSFLVALHSCFQT 418
Cdd:cd06620   2 LKNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIhidaKSSVRKQ------ILRELQILHECHSPYIVSFYGAFLNE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 MDRLYFVMEFVNGGDLmyqiQQVGKFKEPVAVFYAAEIAV----GLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGM 493
Cdd:cd06620  76 NNNIIICMEYMDCGSL----DKILKKKGPFPEEVLGKIAVavleGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 494 CKENIfgDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED-----------ELFTAIT-E 561
Cdd:cd06620 152 SGELI--NSIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmgilDLLQRIVnE 229
                       250       260       270
                ....*....|....*....|....*....|
gi 71986426 562 HNVSYPKS--LSKEAVSLCKALLIKNPSKR 589
Cdd:cd06620 230 PPPRLPKDriFPKDLRDFVDRCLLKDPRER 259
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
104-154 5.94e-20

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 83.65  E-value: 5.94e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71986426   104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLKCSWCKLNVHKRCHEKVPPECG 51
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
354-549 6.35e-20

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 89.72  E-value: 6.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLG--EQKTTKEL-FAIKVLKKDVIIQDDDVecTMTEKRVLALPEKPSFLVALHSCFQTMdrLYFVMEFVN 430
Cdd:cd05060   3 LGHGNFGSVRKGvyLMKSGKEVeVAVKTLKQEHEKAGKKE--FLREASVMAQLDHPCIVRLIGVCKGEP--LMLVMELAP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDA--TTKTFC 508
Cdd:cd05060  79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDyyRATTAG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 71986426 509 GTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05060 159 RWPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGE 201
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
347-547 7.18e-20

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 89.55  E-value: 7.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTV---LGKGSFGKVLLGEQKTTKelFAIKVLKKDVIIQDDDVE-CTMTEKRVLALpeKPSFLVALHscfqtmDRL 422
Cdd:cd05083   4 NLQKLTLgeiIGEGEFGAVLQGEYMGQK--VAVKNIKCDVTAQAFLEEtAVMTKLQHKNL--VRLLGVILH------NGL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG 500
Cdd:cd05083  74 YIVMELMSKGNLVNFLRSRGRALVPVIqlLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71986426 501 DATTKTfcgTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPF 547
Cdd:cd05083 154 VDNSRL---PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
350-609 7.53e-20

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 89.59  E-value: 7.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLG-EQKTTKELfAIKVlkkdviIQDDDVECT-----MTEKRVLALPEKPSFLVALHSCFQT-MDRL 422
Cdd:cd13983   5 FNEVLGRGSFKTVYRAfDTEEGIEV-AWNE------IKLRKLPKAerqrfKQEIEILKSLKHPNIIKFYDSWESKsKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKG--IIYRDLKLDNVMLE-RDGHIKITDFGMCKenIF 499
Cdd:cd13983  78 IFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLAT--LL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATTKTFCGTPDYIAPEiiLYQP-YGKSVDWWAYGVLLFEMLAGQPPFdGEdedelFTAITE--HNVS---YPKSLSKe 573
Cdd:cd13983 156 RQSFAKSVIGTPEFMAPE--MYEEhYDEKVDIYAFGMCLLEMATGEYPY-SE-----CTNAAQiyKKVTsgiKPESLSK- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71986426 574 avslckallIKNPSKR---LGC--TGDDESASRDIKEHPFF 609
Cdd:cd13983 227 ---------VKDPELKdfiEKClkPPDERPSARELLEHPFF 258
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
354-589 8.17e-20

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: 90.46  E-value: 8.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE---------QKTTKelFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYF 424
Cdd:cd05098  21 LGEGCFGQVVLAEaigldkdkpNRVTK--VAVKMLKSDA--TEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQ------------------QVGKFKEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI 486
Cdd:cd05098  97 IVEYASKGNLREYLQarrppgmeycynpshnpeEQLSSKDLVSCAY--QVARGMEYLASKKCIHRDLAARNVLVTEDNVM 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 487 KITDFGMCKENIFGDATTKTFCG--TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-H 562
Cdd:cd05098 175 KIADFGLARDIHHIDYYKKTTNGrlPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKLLKEgH 254
                       250       260
                ....*....|....*....|....*..
gi 71986426 563 NVSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05098 255 RMDKPSNCTNELYMMMRDCWHAVPSQR 281
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
354-582 9.06e-20

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 89.28  E-value: 9.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMD-RLYFVMEFVNGG 432
Cdd:cd14163   8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKN-IIHVYEMLESADgKIYLVMELAEDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDghIKITDFGMCKE-NIFGDATTKTFCGT 510
Cdd:cd14163  87 DVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQgFT--LKLTDFGFAKQlPKGGRELSQTFCGS 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 511 PDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAiTEHNVSYPKSL--SKEAVSLCKALL 582
Cdd:cd14163 165 TAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQ-QQKGVSLPGHLgvSRTCQDLLKRLL 238
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
346-561 1.29e-19

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 89.03  E-value: 1.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKkdviiQDDDVECTMTEKRVLALPE-KPSFLVALHSCFQTMDRLYF 424
Cdd:cd05148   6 EEFTLERKLGSGYFGEVWEGLWKNRVRV-AIKILK-----SDDLLKQQDFQKEVQALKRlRHKHLISLFAVCSVGEPVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQQVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC---KENIF 499
Cdd:cd05148  80 ITELMEKGSLLAFLRSPEGQVLPVAslIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliKEDVY 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426 500 GDATTKtfcgTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE 561
Cdd:cd05148 160 LSSDKK----IPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITA 219
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
351-607 1.53e-19

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 89.64  E-value: 1.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd07870   5 LEKLGEGSYATVYKGISRINGQLVALKVISMKT---EEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd07870  82 TDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVVT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDG-----EDEDELFTAI---TEH---NVSYPKSLSKEAVSLC 578
Cdd:cd07870 162 LWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFPGvsdvfEQLEKIWTVLgvpTEDtwpGVSKLPNYKPEWFLPC 241
                       250       260       270
                ....*....|....*....|....*....|
gi 71986426 579 KALLIKNPSKRLGCTGDDES-ASRDIKEHP 607
Cdd:cd07870 242 KPQQLRVVWKRLSRPPKAEDlASQMLMMFP 271
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
175-260 1.56e-19

C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 84.61  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDP-NGLSDPYVKCKLIPEDSGcKSKQKTKTLRATLNPQWNETFTYKLLPGD-KDRRLSIEVWDWDR 252
Cdd:cd08521  16 LEVHIKECRNLAYADEkKKRSNPYVKVYLLPDKSK-QSKRKTSVKKNTTNPVFNETLKYHISKSQlETRTLQLSVWHHDR 94

                ....*...
gi 71986426 253 TSRNDFMG 260
Cdd:cd08521  95 FGRNTFLG 102
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
350-564 1.77e-19

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 88.59  E-value: 1.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLGEQKttKELFAIKVLKK--DVIIQDDDVEctmTEKRVLALP-EKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd13979   7 LQEPLGSGGFGSVYKATYK--GETVAVKIVRRrrKNRASRQSFW---AELNAARLRhENIVRVLAAETGTDFASLGLIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLmyqiQQV---GKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGmCKENIFG- 500
Cdd:cd13979  82 EYCGNGTL----QQLiyeGSEPLPLAhrILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG-CSVKLGEg 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 501 ---DATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFtAITEHNV 564
Cdd:cd13979 157 nevGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLY-AVVAKDL 222
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
351-609 1.98e-19

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: 88.97  E-value: 1.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKvlkKDVIIQDDDV--ECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEF 428
Cdd:cd07847   6 LSKIGEGSYGVVFKCRNRETGQIVAIK---KFVESEDDPVikKIALREIRMLKQLKHPN-LVNLIEVFRRKRKLHLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFC 508
Cdd:cd07847  82 CDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILYQ-PYGKSVDWWAYGVLLFEMLAGQPPFDGE-DEDELF-------------TAITEHN-----VSYP- 567
Cdd:cd07847 162 ATRWYRAPELLVGDtQYGPPVDVWAIGCVFAELLTGQPLWPGKsDVDQLYlirktlgdliprhQQIFSTNqffkgLSIPe 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71986426 568 -----------KSLSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFF 609
Cdd:cd07847 242 petrepleskfPNISSPALSFLKGCLQMDPTERLSCE--------ELLEHPYF 286
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
351-554 4.46e-19

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 88.14  E-value: 4.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd07871  10 LDKLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GgDLMYQIQQVGKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifgDATTKTFCG 509
Cdd:cd07871  87 S-DLKQYLDNCGNLMSMHNVkIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAK---SVPTKTYSN 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 71986426 510 ---TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDE 554
Cdd:cd07871 163 evvTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKE 211
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
343-572 4.70e-19

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: 87.31  E-value: 4.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVEctmtEKRVLALPEKPSfLVALHS-CFQTMDr 421
Cdd:cd05112   1 IDPSELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAMSEEDFIE----EAEVMMKLSHPK-LVQLYGvCLEQAP- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG 500
Cdd:cd05112  74 ICLVFEFMEHGCLSdYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDD 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 501 DATTKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAI-TEHNVSYPKSLSK 572
Cdd:cd05112 154 QYTSSTGTKFPvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDInAGFRLYKPRLAST 228
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
174-272 4.99e-19

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176007 [Multi-domain]  Cd Length: 121  Bit Score: 83.09  E-value: 4.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLipedsGCKSKQKTKTLRATLNPQWNETFTykLLPGDKDRRLSIEVWDWDRT 253
Cdd:cd04042   1 QLDIHLKEGRNLAARDRGGTSDPYVKFKY-----GGKTVYKSKTIYKNLNPVWDEKFT--LPIEDVTQPLYIKVFDYDRG 73
                        90
                ....*....|....*....
gi 71986426 254 SRNDFMGSLSFGISELMKE 272
Cdd:cd04042  74 LTDDFMGSAFVDLSTLELN 92
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
455-608 5.02e-19

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 88.62  E-value: 5.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 455 EIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGM---CKENIF-GDATTKTFCGTPDYIAPEIIL-YQPYGKSVD 529
Cdd:cd07857 113 QILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLargFSENPGeNAGFMTEYVATRWYRAPEIMLsFQSYTKAID 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 530 WWAYGVLLFEMLAGQPPFDGED----------------EDELFTAITEHNVSYPKSL---------------SKEAVSLC 578
Cdd:cd07857 193 VWSVGCILAELLGRKPVFKGKDyvdqlnqilqvlgtpdEETLSRIGSPKAQNYIRSLpnipkkpfesifpnaNPLALDLL 272
                       170       180       190
                ....*....|....*....|....*....|
gi 71986426 579 KALLIKNPSKRLGCtgddESASrdikEHPF 608
Cdd:cd07857 273 EKLLAFDPTKRISV----EEAL----EHPY 294
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
162-280 5.27e-19

C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176027 [Multi-domain]  Cd Length: 122  Bit Score: 83.11  E-value: 5.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 162 GRLRIEAHIENDQLTIKILEAKNLIPMDpNGLSDPYVKCKLIPeDSGCKSKQKTKTLRATLNPQWNETFTYKLLPGD--K 239
Cdd:cd08381   2 GQVKLSISYKNGTLFVMVMHAKNLPLLD-GSDPDPYVKTYLLP-DPQKTTKRKTKVVRKTRNPTFNEMLVYDGLPVEdlQ 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71986426 240 DRRLSIEVWDWDRTSRNDFMGSLSFGISE--LMKEaASGWYKL 280
Cdd:cd08381  80 QRVLQVSVWSHDSLVENEFLGGVCIPLKKldLSQE-TEKWYPL 121
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
342-549 6.26e-19

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 87.47  E-value: 6.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 342 VIKASDFNFLTVLGKGSFGKVLLG----EQKTTKELFAIKVLKKDVIIQDDdvECTMTEKRVLALPEKPSFLVALHSCFQ 417
Cdd:cd05057   3 IVKETELEKGKVLGSGAFGTVYKGvwipEGEKVKIPVAIKVLREETGPKAN--EEILDEAYVMASVDHPHLVRLLGICLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 TmdRLYFVMEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK- 495
Cdd:cd05057  81 S--QVQLITQLMPLGCLLdYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKl 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 ----ENIFGDATTKtfcgTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05057 159 ldvdEKEYHAEGGK----VPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
354-612 6.46e-19

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 87.95  E-value: 6.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGgD 433
Cdd:PLN00009  10 IGEGTYGVVYKARDRVTNETIALKKIRLEQ--EDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLDL-D 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  434 LMYQIQQVGKF-KEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH-IKITDFGMCKEniFGdATTKTFCG- 509
Cdd:PLN00009  87 LKKHMDSSPDFaKNPRLIkTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARA--FG-IPVRTFTHe 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  510 --TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELF-----------------TAITEHNVSYPK 568
Cdd:PLN00009 164 vvTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEiDELFkifrilgtpneetwpgvTSLPDYKSAFPK 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426  569 -----------SLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFFRRI 612
Cdd:PLN00009 244 wppkdlatvvpTLEPAGVDLLSKMLRLDPSKRI--------TARAALEHEYFKDL 290
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
354-547 7.80e-19

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 86.52  E-value: 7.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDviIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDrLYFVMEFVNGGD 433
Cdd:cd05084   4 IGRGNFGEVFSGRLRADNTPVAVKSCRET--LPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQP-IYIVMELVQGGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVG---KFKEPVAVfyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG-DATTKTFCG 509
Cdd:cd05084  81 FLTFLRTEGprlKVKELIRM--VENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGvYAATGGMKQ 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 71986426 510 TP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPF 547
Cdd:cd05084 159 IPvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPY 198
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
354-561 8.52e-19

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: 87.02  E-value: 8.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELfAIKVLKKDVIiqddDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd05072  15 LGAGQFGEVWMGYYNNSTKV-AVKTLKPGTM----SVQAFLEEANLMKTLQHDK-LVRLYAVVTKEEPIYIITEYMAKGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LM--YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05072  89 LLdfLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFP 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 512 -DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE 561
Cdd:cd05072 169 iKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQR 220
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
462-611 8.62e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 88.00  E-value: 8.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 462 FLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK------ENIFGDATTktfcgtpDYIA------PEIILYQP-YGKSV 528
Cdd:cd07852 122 YLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARslsqleEDDENPVLT-------DYVAtrwyraPEILLGSTrYTKGV 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 529 DWWAYGVLLFEMLAGQPPFDG-------------------EDEDEL---FTA--ITEHNVSYPKSL-------SKEAVSL 577
Cdd:cd07852 195 DMWSVGCILGEMLLGKPLFPGtstlnqlekiievigrpsaEDIESIqspFAAtmLESLPPSRPKSLdelfpkaSPDALDL 274
                       170       180       190
                ....*....|....*....|....*....|....
gi 71986426 578 CKALLIKNPSKRLGCtgddESASRdikeHPFFRR 611
Cdd:cd07852 275 LKKLLVFNPNKRLTA----EEALR----HPYVAQ 300
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
421-591 9.10e-19

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: 86.26  E-value: 9.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH---IKITDFGMCKE- 496
Cdd:cd14012  78 KVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTl 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 -NIFGDATTKTFCGTPdYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFdgededELFTaiTEHNVSYPKSLSKEA 574
Cdd:cd14012 158 lDMCSRGSLDEFKQTY-WLPPELAQgSKSPTRKTDVWDLGLLFLQMLFGLDVL------EKYT--SPNPVLVSLDLSASL 228
                       170
                ....*....|....*..
gi 71986426 575 VSLCKALLIKNPSKRLG 591
Cdd:cd14012 229 QDFLSKCLSLDPKKRPT 245
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
422-561 1.00e-18

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: 88.01  E-value: 1.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVnGGDLmYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeniFGD 501
Cdd:cd07856  85 IYFVTELL-GTDL-HRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR---IQD 159
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426 502 ATTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd07856 160 PQMTGYVSTRYYRAPEIMLtWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITE 220
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
354-609 1.10e-18

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: 86.11  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVlkkdVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGgD 433
Cdd:cd14108  10 IGRGAFSYLRRVKEKSSDLSFAAKF----IPVRAKKKTSARRELALLAELDHKS-IVRFHDAFEKRRVVIIVTELCHE-E 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG--HIKITDFGMCKENIFGDattKTFC--G 509
Cdd:cd14108  84 LLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNE---PQYCkyG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP----KSLSKEAVSLCKALLIKN 585
Cdd:cd14108 161 TPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEesmfKDLCREAKGFIIKVLVSD 240
                       250       260
                ....*....|....*....|....
gi 71986426 586 pskRLGCTGDdesasrDIKEHPFF 609
Cdd:cd14108 241 ---RLRPDAE------ETLEHPWF 255
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
351-608 1.32e-18

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: 86.50  E-value: 1.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKV--LLGEQKttkELFAIKVlkkdVIIQDDDVECTMTEKRVLALPEKPSF---LVAL--HSCFQTMDRLY 423
Cdd:cd14131   6 LKQLGKGGSSKVykVLNPKK---KIYALKR----VDLEGADEQTLQSYKNEIELLKKLKGsdrIIQLydYEVTDEDDYLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFvNGGDL--MYQIQQVGKFKEPVAVFYAAEI--AVGlfFLHSKGIIYRDLKLDNVMLErDGHIKITDFGMCKeNIF 499
Cdd:cd14131  79 MVMEC-GEIDLatILKKKRPKPIDPNFIRYYWKQMleAVH--TIHEEGIVHSDLKPANFLLV-KGRLKLIDFGIAK-AIQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATT---KTFCGTPDYIAPEIIL---YQPYGKSV-------DWWAYGVLLFEMLAGQPPFdGEDEDEL--FTAITE--H 562
Cdd:cd14131 154 NDTTSivrDSQVGTLNYMSPEAIKdtsASGEGKPKskigrpsDVWSLGCILYQMVYGKTPF-QHITNPIakLQAIIDpnH 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71986426 563 NVSYPKSLSKEAVSLCKALLIKNPSKRLgctgddesasrDIKE---HPF 608
Cdd:cd14131 233 EIEFPDIPNPDLIDVMKRCLQRDPKKRP-----------SIPEllnHPF 270
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
348-555 1.35e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 86.77  E-value: 1.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVME 427
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLD---AEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGgDLMYQIQQVGKFK--EPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGdATT 504
Cdd:cd07836  79 YMDK-DLKKYMDTHGVRGalDPNTVkSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARA--FG-IPV 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 505 KTFCG---TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED-EDEL 555
Cdd:cd07836 155 NTFSNevvTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNnEDQL 210
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
351-609 1.38e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 86.98  E-value: 1.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd07873   7 LDKLGEGTYATVYKGRSKLTDNLVALKEIRLE---HEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GgDLMYQIQQVGKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCG 509
Cdd:cd07873  84 K-DLKQYLDDCGNSINMHNVkLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI-----TEHNVSYPKSLSKEAVS------- 576
Cdd:cd07873 163 TLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIfrilgTPTEETWPGILSNEEFKsynypky 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71986426 577 LCKALLIKNP----------SKRLGCTGDDESASRDIKEHPFF 609
Cdd:cd07873 243 RADALHNHAPrldsdgadllSKLLQFEGRKRISAEEAMKHPYF 285
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
352-608 1.54e-18

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 85.79  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDV-ECTMTEKRVLALPEKPSF---LVALHSCFQTMDRLYFVME 427
Cdd:cd14100   6 PLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELpNGTRVPMEIVLLKKVGSGfrgVIRLLDWFERPDSFVLVLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNG-GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDGHIKITDFG---MCKENIFGDa 502
Cdd:cd14100  86 RPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGsgaLLKDTVYTD- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 ttktFCGTPDYIAPEIILYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEdelftaITEHNVSYPKSLSKEAVSLCKAL 581
Cdd:cd14100 165 ----FDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFFRQRVSSECQHLIKWC 234
                       250       260
                ....*....|....*....|....*..
gi 71986426 582 LIKNPSkrlgctgdDESASRDIKEHPF 608
Cdd:cd14100 235 LALRPS--------DRPSFEDIQNHPW 253
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
409-589 1.55e-18

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 86.22  E-value: 1.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 409 LVALHSCFQT-MDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFL--HSKGIIYRDLKLDNVMLERD-- 483
Cdd:cd13990  66 IVKLYDVFEIdTDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGnv 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 484 -GHIKITDFGMCK---ENIFGDAT---TKTFCGTPDYIAPEIILYQPYGKS----VDWWAYGVLLFEMLAGQPPFdGED- 551
Cdd:cd13990 146 sGEIKITDFGLSKimdDESYNSDGmelTSQGAGTYWYLPPECFVVGKTPPKisskVDVWSVGVIFYQMLYGRKPF-GHNq 224
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 71986426 552 --EDELF--TAITEHNVSYPK--SLSKEAVSLCKALLIKNPSKR 589
Cdd:cd13990 225 sqEAILEenTILKATEVEFPSkpVVSSEAKDFIRRCLTYRKEDR 268
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
418-643 2.09e-18

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 87.31  E-value: 2.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 TMDRL---YFVMEFVnGGDLMyQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC 494
Cdd:cd07880  88 SLDRFhdfYLVMPFM-GTDLG-KLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 KENifgDATTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI-------------- 559
Cdd:cd07880 166 RQT---DSEMTGYVVTRWYRAPEVILnWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEImkvtgtpskefvqk 242
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 560 --TEHNVSYPKSLSK---------------EAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFFRRIDWFKIETrQI 622
Cdd:cd07880 243 lqSEDAKNYVKKLPRfrkkdfrsllpnanpLAVNVLEKMLVLDAESRITAA--------EALAHPYFEEFHDPEDET-EA 313
                       250       260
                ....*....|....*....|.
gi 71986426 623 QPpfkpklktdrstenFDHSF 643
Cdd:cd07880 314 PP--------------YDDSF 320
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
354-611 2.10e-18

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: 86.63  E-value: 2.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG- 432
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPN-TIEYKGCYLKDHTAWLVMEYCLGSa 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 -DLMYQIQQVGKFKEPVAVFYAAeiAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifgdATTKTFCGTP 511
Cdd:cd06633 108 sDLLEVHKKPLQEVEIAAITHGA--LQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA----SPANSFVGTP 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 DYIAPEIILYQPYGK---SVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLS-----KEAVSLCkalLI 583
Cdd:cd06633 182 YWMAPEVILAMDEGQydgKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNEwtdsfRGFVDYC---LQ 258
                       250       260
                ....*....|....*....|....*...
gi 71986426 584 KNPSKRLgctgddesASRDIKEHPFFRR 611
Cdd:cd06633 259 KIPQERP--------SSAELLRHDFVRR 278
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
351-555 2.31e-18

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: 86.58  E-value: 2.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd07872  11 LEKLGEGTYATVFKGRSKLTENLVALKEIRLE---HEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GgDLMYQIQQVGKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifgDATTKTFCG 509
Cdd:cd07872  88 K-DLKQYMDDCGNIMSMHNVkIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAK---SVPTKTYSN 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 510 ---TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED-EDEL 555
Cdd:cd07872 164 evvTLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTvEDEL 214
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
353-589 2.50e-18

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 85.74  E-value: 2.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTtkELFAIKVLKK-----------DVIIQDDDVECTMT-------EKRVLALPEKPSFLVALHS 414
Cdd:cd14000   1 LLGDGGFGSVYRASYKG--EPVAVKIFNKhtssnfanvpaDTMLRHLRATDAMKnfrllrqELTVLSHLHHPSIVYLLGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 415 CFQTmdrLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFY----AAEIAVGLFFLHSKGIIYRDLKLDNVML-----ERDGH 485
Cdd:cd14000  79 GIHP---LMLVLELAPLGSLDHLLQQDSRSFASLGRTLqqriALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 486 IKITDFGMCKENIFGDAttKTFCGTPDYIAPEIILYQ-PYGKSVDWWAYGVLLFEMLAGQPPFDGedEDELFTAITEHNV 564
Cdd:cd14000 156 IKIADYGISRQCCRMGA--KGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVG--HLKFPNEFDIHGG 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 71986426 565 SYPKSLSKEAV--SLCKALLIK----NPSKR 589
Cdd:cd14000 232 LRPPLKQYECApwPEVEVLMKKcwkeNPQQR 262
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
355-589 2.75e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 84.62  E-value: 2.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 355 GKGSFGKVLLGEQKTTKELFAIKVLKKdvIIQDDDVECTMTEKRVL----ALPEKPSFLVALHscFQTMDRLYfvmEFVN 430
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK--IEKEAEILSVLSHRNIIqfygAILEAPNYGIVTE--YASYGSLF---DYLN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDL----MYQIQQvgkfkepvavfYAAEIAVGLFFLHSKG---IIYRDLKLDNVMLERDGHIKITDFGMCKenIFGDAT 503
Cdd:cd14060  75 SNESeemdMDQIMT-----------WATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTT 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHN--VSYPKSLSKEAVSLCKAL 581
Cdd:cd14060 142 HMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNerPTIPSSCPRSFAELMRRC 221

                ....*...
gi 71986426 582 LIKNPSKR 589
Cdd:cd14060 222 WEADVKER 229
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
177-261 3.08e-18

C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176002 [Multi-domain]  Cd Length: 124  Bit Score: 81.06  E-value: 3.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 177 IKILEAKNLIPMDPNGLSDPYVKCKLipedSGCKSKQKTKTLRATLNPQWNETFTYK-LLPGDKDrrLSIEVWDWDRTSR 255
Cdd:cd04037   4 VYVVRARNLQPKDPNGKSDPYLKIKL----GKKKINDRDNYIPNTLNPVFGKMFELEaTLPGNSI--LKISVMDYDLLGS 77

                ....*.
gi 71986426 256 NDFMGS 261
Cdd:cd04037  78 DDLIGE 83
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
175-265 3.58e-18

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 81.32  E-value: 3.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCkSKQKTKTLRATLNPQWNETFTYKlLPGDKDRRLSIE--VWDWDR 252
Cdd:cd08404  17 LTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRI-SKKKTHVKKCTLNPVFNESFVFD-IPSEELEDISVEflVLDSDR 94
                        90
                ....*....|...
gi 71986426 253 TSRNDFMGSLSFG 265
Cdd:cd08404  95 VTKNEVIGRLVLG 107
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
343-565 3.95e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 85.88  E-value: 3.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDV--IIQDDDVEctmtEKRVLALPEKPsFLVALHSCFQTMD 420
Cdd:cd06650   2 LKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIkpAIRNQIIR----ELQVLHECNSP-YIVGFYGAFYSDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCKENIf 499
Cdd:cd06650  77 EISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI- 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 500 gDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQ---PPFDGEDEDELFTAITEHNVS 565
Cdd:cd06650 156 -DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRypiPPPDAKELELMFGCQVEGDAA 223
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
337-612 4.15e-18

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: 85.08  E-value: 4.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 337 SSNHNVIKASDFNFLTVLGKGSFGKVLLGEQKTTkelFAIKVLKkdviIQDDDVECTMTEKRVLALPEKPSFL-VALHSC 415
Cdd:cd14149   3 SSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGD---VAVKILK----VVDPTPEQFQAFRNEVAVLRKTRHVnILLFMG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 416 FQTMDRLYFVMEFVNGGDLMYQIQ-QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC 494
Cdd:cd14149  76 YMTKDNLAIVTQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 --KENIFGDATTKTFCGTPDYIAPEIILYQ---PYGKSVDWWAYGVLLFEMLAGQPPFDG-EDEDELFTAITEHNVSypK 568
Cdd:cd14149 156 tvKSRWSGSQQVEQPTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPYSHiNNRDQIIFMVGRGYAS--P 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71986426 569 SLSKEAVSLCKALliknpsKRLgcTGDDESASRDikEHPFFRRI 612
Cdd:cd14149 234 DLSKLYKNCPKAM------KRL--VADCIKKVKE--ERPLFPQI 267
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
161-280 4.19e-18

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 80.78  E-value: 4.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 161 RGRLRIEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPeDSGCKSKQKTKTLRATLNPQWNETFTYKL-LPGDK 239
Cdd:cd04030   4 RIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLP-DKSKSTRRKTSVKKDNLNPVFDETFEFPVsLEELK 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71986426 240 DRRLSIEVwdwdRTSR------NDFMGSLSFGISEL-MKEAASGWYKL 280
Cdd:cd04030  83 RRTLDVAV----KNSKsflsreKKLLGQVLIDLSDLdLSKGFTQWYDL 126
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
351-634 4.81e-18

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 86.11  E-value: 4.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKK----DVIIQDDDVECT----MTEKRVLALPEKPSFLVALHScfqtMDRL 422
Cdd:cd07879  20 LKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRpfqsEIFAKRAYRELTllkhMQHENVIGLLDVFTSAVSGDE----FQDF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFvnggdLMYQIQQV--GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnifG 500
Cdd:cd07879  96 YLVMPY-----MQTDLQKImgHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARH---A 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 DATTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE----------------HN 563
Cdd:cd07879 168 DAEMTGYVVTRWYRAPEVILnWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKvtgvpgpefvqkledkAA 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 564 VSYPKSL---------------SKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFFrriDWFK-IETRQIQPPFK 627
Cdd:cd07879 248 KSYIKSLpkyprkdfstlfpkaSPQAVDLLEKMLELDVDKRLTAT--------EALEHPYF---DSFRdADEETEQQPYD 316

                ....*..
gi 71986426 628 PKLKTDR 634
Cdd:cd07879 317 DSLENEK 323
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
354-589 6.26e-18

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 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 FGFR3 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: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 85.46  E-value: 6.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE------QKTTKEL-FAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05100  20 LGEGCFGQVVMAEaigidkDKPNKPVtVAVKMLKDDA--TDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQI------------------QQVGKFKEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI 488
Cdd:cd05100  98 EYASKGNLREYLrarrppgmdysfdtcklpEEQLTFKDLVSCAY--QVARGMEYLASQKCIHRDLAARNVLVTEDNVMKI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 489 TDFGMCKENIFGDATTKTFCG--TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNV 564
Cdd:cd05100 176 ADFGLARDVHNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEgHRM 255
                       250       260
                ....*....|....*....|....*
gi 71986426 565 SYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05100 256 DKPANCTHELYMIMRECWHAVPSQR 280
C2_RGS-like cd08685
C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of ...
162-280 6.39e-18

C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of the regulator of G-protein signaling (RGS) family. RGS is a GTPase activating protein which inhibits G-protein mediated signal transduction. The protein is largely cytosolic, but G-protein activation leads to translocation of this protein to the plasma membrane. A nuclear form of this protein has also been described, but its sequence has not been identified. There are multiple alternatively spliced transcript variants in this family with some members having additional domains (ex. PDZ and RGS) downstream of the C2 domain. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176067 [Multi-domain]  Cd Length: 119  Bit Score: 80.19  E-value: 6.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 162 GRLRIEAHIENDQLTIKILEAKNLIPMDPNGlSDPYVKCKLIPEDsGCKSKQKTKTLRATLNPQWNETFTYKLLPGDKDR 241
Cdd:cd08685   1 GQLKLSIEGQNRKLTLHVLEAKGLRSTNSGT-CNSYVKISLSPDK-EVRFRQKTSTVPDSANPLFHETFSFDVNERDYQK 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71986426 242 RLSIEVWDWDRTSRND-FMGSLSFGI-SELMKEAASGWYKL 280
Cdd:cd08685  79 RLLVTVWNKLSKSRDSgLLGCMSFGVkSIVNQKEISGWYYL 119
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
432-609 6.84e-18

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 83.55  E-value: 6.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLeRDGHIKITDFGMCKENIFGDATTKTFC--- 508
Cdd:cd14022  69 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVF-KDEERTRVKLESLEDAYILRGHDDSLSdkh 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEII-LYQPY-GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSLCKALLIKNP 586
Cdd:cd14022 148 GCPAYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREP 227
                       170       180
                ....*....|....*....|...
gi 71986426 587 SKRLgctgddesASRDIKEHPFF 609
Cdd:cd14022 228 SERL--------TSQEILDHPWF 242
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
409-609 7.84e-18

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 83.72  E-value: 7.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 409 LVALHSCFQTMDR-LYFVMEFVNGGDLMYQ--IQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDgH 485
Cdd:cd14109  58 IVQMHDAYDDEKLaVTVIDNLASTIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-K 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 486 IKITDFGMCKENIFGDATTKTFcGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVS 565
Cdd:cd14109 137 LKLADFGQSRRLLRGKLTTLIY-GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWS 215
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 566 YPKS----LSKEAVSLCKALLIKNPSKRLgctgddesasrDIKE---HPFF 609
Cdd:cd14109 216 FDSSplgnISDDARDFIKKLLVYIPESRL-----------TVDEalnHPWF 255
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
345-541 9.48e-18

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: 84.16  E-value: 9.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKvlkkDVIIQDDDV--ECTMTEKRVLALPEKPSFLVALHSCFQT---- 418
Cdd:cd14048   5 LTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVK----RIRLPNNELarEKVLREVRALAKLDHPGIVRYFNAWLERppeg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 ----MDR--LYFVMEFV---NGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKIT 489
Cdd:cd14048  81 wqekMDEvyLYIQMQLCrkeNLKDWMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426 490 DFGMC------------KENIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEML 541
Cdd:cd14048 161 DFGLVtamdqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
346-613 1.02e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 84.41  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDV-------IIQdddvectmtEKRVLALPEKPsFLVALHSCFQT 418
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIkpairnqIIR---------ELKVLHECNSP-YIVGFYGAFYS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 MDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCKEN 497
Cdd:cd06615  71 DGEISICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IfgDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDEL----------------FTAITE 561
Cdd:cd06615 151 I--DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELeamfgrpvsegeakesHRPVSG 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 562 HNVSYPKSL----------------------SKEAVSLCKALLIKNPSKRLgctgddesasrDIKE---HPFFRRID 613
Cdd:cd06615 229 HPPDSPRPMaifelldyivnepppklpsgafSDEFQDFVDKCLKKNPKERA-----------DLKEltkHPFIKRAE 294
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
357-609 1.14e-17

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 84.20  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 357 GSFGKVLLGEQKTTKELFAIKVLKkdviiqdddvectMTEKR----VLALPEKPSFLVALHSCF---------QTMDRLY 423
Cdd:cd07843  16 GTYGVVYRARDKKTGEIVALKKLK-------------MEKEKegfpITSLREINILLKLQHPNIvtvkevvvgSNLDKIY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGG--DLMYQiqqvgkFKEPvavFYAAEIAV-------GLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC 494
Cdd:cd07843  83 MVMEYVEHDlkSLMET------MKQP---FLQSEVKClmlqllsGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 495 KEniFGDATTKTfcgTPD-----YIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELF----------- 556
Cdd:cd07843 154 RE--YGSPLKPY---TQLvvtlwYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEiDQLNkifkllgtpte 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986426 557 --------------TAITEHNVSY------PKSLSKEAVSLCKALLIKNPSKRLgctgddeSASrDIKEHPFF 609
Cdd:cd07843 229 kiwpgfselpgakkKTFTKYPYNQlrkkfpALSLSDNGFDLLNRLLTYDPAKRI-------SAE-DALKHPYF 293
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
348-611 1.36e-17

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: 83.27  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLK----------KDVIiqdddvectmteKRVLALPE-KPSFLVALHSCF 416
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSysgkqstekwQDII------------KEVKFLRQlRHPNTIEYKGCY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDRLYFVMEFVNGGdlMYQIQQVgkFKEPVavfYAAEIAV-------GLFFLHSKGIIYRDLKLDNVMLERDGHIKIT 489
Cdd:cd06607  71 LREHTAWLVMEYCLGS--ASDIVEV--HKKPL---QEVEIAAichgalqGLAYLHSHNRIHRDVKAGNILLTEPGTVKLA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 490 DFG----MCKENifgdattkTFCGTPDYIAPEIILYQ---PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEH 562
Cdd:cd06607 144 DFGsaslVCPAN--------SFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQN 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 563 NvsyPKSL-----SKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFFRR 611
Cdd:cd06607 216 D---SPTLssgewSDDFRNFVDSCLQKIPQDR--------PSAEDLLKHPFVTR 258
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
346-561 1.45e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 84.76  E-value: 1.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKD-VIIQDDDVECTMTEKRVLALPEKPSFlVALHSCFQTMDRLYF 424
Cdd:cd14228  15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHpSYARQGQIEVSILSRLSSENADEYNF-VRSYECFQHKNHTCL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGdlMYQIQQVGKFkEPVAVFYA----AEIAVGLFFLHSKGIIYRDLKLDNVML----ERDGHIKITDFGMCKE 496
Cdd:cd14228  94 VFEMLEQN--LYDFLKQNKF-SPLPLKYIrpilQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 497 niFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14228 171 --VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQ 233
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
346-589 1.62e-17

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 83.36  E-value: 1.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviIQDDDVECTMTEKRVLALPEKPsFLVALHSCFQTMDRLYFV 425
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLE--LDESKFNQIIMELDILHKAVSP-YIVDFYGAFFIEGAVYMC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGG--DLMY-QIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCKENIfgD 501
Cdd:cd06622  78 MEYMDAGslDKLYaGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV--A 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTKTFCGTPDYIAPEIILYQ------PYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELF---TAITEHN-VSYPKSLS 571
Cdd:cd06622 156 SLAKTNIGCQSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaqlSAIVDGDpPTLPSGYS 235
                       250
                ....*....|....*...
gi 71986426 572 KEAVSLCKALLIKNPSKR 589
Cdd:cd06622 236 DDAQDFVAKCLNKIPNRR 253
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
160-269 1.68e-17

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 79.32  E-value: 1.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 160 KRGRL--RIEAHIENDQLTIKILEAKNLIPMDP-NGLSDPYVKCKLIPEDsgcKSKQKTKTLRATLNPQWNETFTYKLLP 236
Cdd:cd08388   1 KLGTLffSLRYNSEKKALLVNIIECRDLPAMDEqSGTSDPYVKLQLLPEK---EHKVKTRVLRKTRNPVYDETFTFYGIP 77
                        90       100       110
                ....*....|....*....|....*....|....*
gi 71986426 237 GDKDRRLSIE--VWDWDRTSRNDFMGSLSFGISEL 269
Cdd:cd08388  78 YNQLQDLSLHfaVLSFDRYSRDDVIGEVVCPLAGA 112
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
351-642 3.01e-17

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 83.56  E-value: 3.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKK--DVIIQdddVECTMTEKRVLAlPEKPSFLVALHSCF------QTMDRL 422
Cdd:cd07878  20 LTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSLIH---ARRTYRELRLLK-HMKHENVIGLLDVFtpatsiENFNEV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVnGGDLmYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnifGDA 502
Cdd:cd07878  96 YLVTNLM-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ---ADD 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 TTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED---------------EDELFTAI-TEHNVS 565
Cdd:cd07878 171 EMTGYVATRWYRAPEIMLnWMHYNQTVDIWSVGCIMAELLKGKALFPGNDyidqlkrimevvgtpSPEVLKKIsSEHARK 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 566 YPKSL---------------SKEAVSLCKALLIKNPSKRLgctgddeSASRDIKeHPFFrrIDWFKIETRQIQPPFkpkl 630
Cdd:cd07878 251 YIQSLphmpqqdlkkifrgaNPLAIDLLEKMLVLDSDKRI-------SASEALA-HPYF--SQYHDPEDEPEAEPY---- 316
                       330
                ....*....|..
gi 71986426 631 ktDRSTENFDHS 642
Cdd:cd07878 317 --DESPENKERT 326
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
348-589 3.53e-17

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 81.89  E-value: 3.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdviIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIP----YKPEDKQLVLREYQVLRRLSHPR-IAQLHSAYLSPRHLVLIEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTF 507
Cdd:cd14110  80 LCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 508 CGtpDYI---APEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPK---SLSKEAVSLCKAL 581
Cdd:cd14110 160 KG--DYVetmAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRcyaGLSGGAVNFLKST 237

                ....*...
gi 71986426 582 LIKNPSKR 589
Cdd:cd14110 238 LCAKPWGR 245
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
432-609 3.59e-17

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 81.32  E-value: 3.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKL----------DNVMLE--RDGHIKITDfgmckenif 499
Cdd:cd13976  69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLrkfvfadeerTKLRLEslEDAVILEGE--------- 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 gDATTKTFCGTPDYIAPEIILYQPY--GKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEAVSL 577
Cdd:cd13976 140 -DDSLSDKHGCPAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCL 218
                       170       180       190
                ....*....|....*....|....*....|..
gi 71986426 578 CKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd13976 219 IRSLLRREPSERL--------TAEDILLHPWL 242
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
350-541 3.64e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 82.43  E-value: 3.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLG----EQKTTKELFAIKVLKKD-VIIQDDDVECTMTEKRVLALPekpsFLVALHSCFQTMDR--L 422
Cdd:cd05038   8 FIKQLGEGHFGSVELCrydpLGDNTGEQVAVKSLQPSgEEQHMSDFKREIEILRTLDHE----YIVKYKGVCESPGRrsL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQ-QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKeniFGD 501
Cdd:cd05038  84 RLIMEYLPSGSLRDYLQrHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK---VLP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 71986426 502 ATTKTFCGTPD------YIAPEIILYQPYGKSVDWWAYGVLLFEML 541
Cdd:cd05038 161 EDKEYYYVKEPgespifWYAPECLRESRFSSASDVWSFGVTLYELF 206
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
354-589 3.88e-17

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 82.70  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE----QKTTKE---LFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05099  20 LGEGCFGQVVRAEaygiDKSRPDqtvTVAVKMLKDNA--TDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPLYVIV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGG--------------DLMYQIQQVGK----FKEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI 488
Cdd:cd05099  98 EYAAKGnlreflrarrppgpDYTFDITKVPEeqlsFKDLVSCAY--QVARGMEYLESRRCIHRDLAARNVLVTEDNVMKI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 489 TDFGMCKENIFGDATTKTFCG-TP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNV 564
Cdd:cd05099 176 ADFGLARGVHDIDYYKKTSNGrLPvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFKLLREgHRM 255
                       250       260
                ....*....|....*....|....*
gi 71986426 565 SYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05099 256 DKPSNCTHELYMLMRECWHAVPTQR 280
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
344-549 3.90e-17

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 82.82  E-value: 3.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 344 KASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLY 423
Cdd:cd07869   3 KADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR---LQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd07869  80 LVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71986426 504 TKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDG 549
Cdd:cd07869 160 YSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPG 206
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
348-552 4.04e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 83.15  E-value: 4.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKD-VIIQDDDVECTMTEKrvLALPEKPSF-LVALHSCFQTMDRLYFV 425
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHpSYARQGQIEVGILAR--LSNENADEFnFVRAYECFQHRNHTCLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGdlMYQIQQVGKFKE-PVAVFYA--AEIAVGLFFLHSKGIIYRDLKLDNVML----ERDGHIKITDFGMCKEni 498
Cdd:cd14229  80 FEMLEQN--LYDFLKQNKFSPlPLKVIRPilQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASH-- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 499 fgdaTTKTFCGT----PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE 552
Cdd:cd14229 156 ----VSKTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALE 209
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
39-88 4.43e-17

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 75.20  E-value: 4.43e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 71986426     39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
348-561 4.61e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 83.22  E-value: 4.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKD-VIIQDDDVECTMTEKRVLALPEKPSFLVAlHSCFQTMDRLYFVM 426
Cdd:cd14227  17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHpSYARQGQIEVSILARLSTESADDYNFVRA-YECFQHKNHTCLVF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGdlMYQIQQVGKFkEPVAVFYA----AEIAVGLFFLHSKGIIYRDLKLDNVML----ERDGHIKITDFGMCKEni 498
Cdd:cd14227  96 EMLEQN--LYDFLKQNKF-SPLPLKYIrpilQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASH-- 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986426 499 FGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14227 171 VSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQ 233
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
344-594 5.02e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 85.56  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   344 KASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL--------KKDVIIQDDDVECTMTEKRVLALPEKpsFLValhsc 415
Cdd:PTZ00266   11 RLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIsyrglkerEKSQLVIEVNVMRELKHKNIVRYIDR--FLN----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   416 fQTMDRLYFVMEFVNGGDLMYQIQQV----GKFKEPVAVFYAAEIAVGLFFLHS-------KGIIYRDLKLDNVMLERD- 483
Cdd:PTZ00266   84 -KANQKLYILMEFCDAGDLSRNIQKCykmfGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426   484 GHI----------------KITDFGMCKeNIFGDATTKTFCGTPDYIAPEIILYQ--PYGKSVDWWAYGVLLFEMLAGQP 545
Cdd:PTZ00266  163 RHIgkitaqannlngrpiaKIGDFGLSK-NIGIESMAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKT 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71986426   546 PFDGEDEDELFTAITEHNVSYP-KSLSKEAVSLCKALLIKNPSKR---LGCTG 594
Cdd:PTZ00266  242 PFHKANNFSQLISELKRGPDLPiKGKSKELNILIKNLLNLSAKERpsaLQCLG 294
pknD PRK13184
serine/threonine-protein kinase PknD;
354-551 5.31e-17

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 85.59  E-value: 5.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIiqdddvECTMTEKRVLALPEKPSFL-----VALHSCFQTMDRLYFVMEF 428
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRVALKKIREDLS------ENPLLKKRFLREAKIAADLihpgiVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  429 VNGGDL------MYQIQQVGK---FKEPVAVFYAA--EIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK-- 495
Cdd:PRK13184  84 IEGYTLksllksVWQKESLSKelaEKTSVGAFLSIfhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIfk 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986426  496 -----ENIFGDATTKTFC-----------GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:PRK13184 164 kleeeDLLDIDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKK 235
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
342-589 5.31e-17

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: 81.24  E-value: 5.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 342 VIKASDFNFLTVLGKGSFGKVLLGEQKTTKelFAIKVLKKDviiqDDDVECTMTEKRVLALPEKPSFLVALHSCFQTmDR 421
Cdd:cd05039   2 AINKKDLKLGELIGKGEFGDVMLGDYRGQK--VAVKCLKDD----STAAQAFLAEASVMTTLRHPNLVQLLGVVLEG-NG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNGGDLMYQIQQVGK----FKEPVAvfYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEN 497
Cdd:cd05039  75 LYIVTEYMAKGSLVDYLRSRGRavitRKDQLG--FALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IFGDATTKtfcgTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNVSYPKSLSKEA 574
Cdd:cd05039 153 SSNQDGGK----LPiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPHVEKgYRMEAPEGCPPEV 228
                       250
                ....*....|....*
gi 71986426 575 VSLCKALLIKNPSKR 589
Cdd:cd05039 229 YKVMKNCWELDPAKR 243
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
354-589 5.41e-17

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: 82.37  E-value: 5.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE-----QKTTKE--LFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05101  32 LGEGCFGQVVMAEavgidKDKPKEavTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIV 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLM--------------YQIQQVGK----FKEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI 488
Cdd:cd05101 110 EYASKGNLReylrarrppgmeysYDINRVPEeqmtFKDLVSCTY--QLARGMEYLASQKCIHRDLAARNVLVTENNVMKI 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 489 TDFGMCKENIFGDATTKTFCG--TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNV 564
Cdd:cd05101 188 ADFGLARDINNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKLLKEgHRM 267
                       250       260
                ....*....|....*....|....*
gi 71986426 565 SYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05101 268 DKPANCTNELYMMMRDCWHAVPSQR 292
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
348-552 5.44e-17

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 82.50  E-value: 5.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDV----IIQdddVECTMTEKRVLALPEKPSFLVALHsCFQTMDRLY 423
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPsyarQGQ---IEVSILSRLSQENADEFNFVRAYE-CFQHKNHTC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGdlMYQIQQVGKFKePVAVFY----AAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG----HIKITDFGmcK 495
Cdd:cd14211  77 LVFEMLEQN--LYDFLKQNKFS-PLPLKYirpiLQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFG--S 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 496 ENIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE 552
Cdd:cd14211 152 ASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSE 208
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
354-605 5.83e-17

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 81.40  E-value: 5.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEC-TMTEKRVL----ALPEKPSFLValhscfqtmdrlyfVMEF 428
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACaGLTSPRVVplygAVREGPWVNI--------------FMDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG-HIKITDFGMcKENIFGDATTKT- 506
Cdd:cd13991  80 KEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGH-AECLDPDGLGKSl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 507 -----FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAItehnVSYPKSLsKEAVSLC--- 578
Cdd:cd13991 159 ftgdyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKI----ANEPPPL-REIPPSCapl 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 71986426 579 -----KALLIKNPSKRLGCTGDDESASRDIKE 605
Cdd:cd13991 234 taqaiQAGLRKEPVHRASAAELRRKTNRALQE 265
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
348-589 5.85e-17

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: 81.42  E-value: 5.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTK--ELFAIKVL----KKDVIIQDDDVECTMTEKRVLALpekpsflvalHSCFQTMDR 421
Cdd:cd14112   5 FSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVKIFevsdEASEAVREFESLRTLQHENVQRL----------IAAFKPSNF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNGgDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLE--RDGHIKITDFGMCKEniF 499
Cdd:cd14112  75 AYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQK--V 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATTKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDElftAITEHNVSY--------PKSL 570
Cdd:cd14112 152 SKLGKVPVDGDTDWASPEFHNpETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDE---EETKENVIFvkcrpnliFVEA 228
                       250
                ....*....|....*....
gi 71986426 571 SKEAVSLCKALLIKNPSKR 589
Cdd:cd14112 229 TQEALRFATWALKKSPTRR 247
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
104-153 5.94e-17

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 75.03  E-value: 5.94e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20795   4 HSLFVHSYKSPTFCDFCGEMLFGLVRQGLKCEGCGLNFHKRCAYKIPNNC 53
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
354-591 6.14e-17

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 81.16  E-value: 6.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLG--EQKTTKELFAIKVLKK---DVIIQDDdvecTMTEKRVLALPEKPSFLVALHSCfqTMDRLYFVMEF 428
Cdd:cd05116   3 LGSGNFGTVKKGyyQMKKVVKTVAVKILKNeanDPALKDE----LLREANVMQQLDNPYIVRMIGIC--EAESWMLVMEM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK-----ENIFGDAT 503
Cdd:cd05116  77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKalradENYYKAQT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFcgtP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNVSYPKSLSKEAVSLCKA 580
Cdd:cd05116 157 HGKW---PvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKgERMECPAGCPPEMYDLMKL 233
                       250
                ....*....|.
gi 71986426 581 LLIKNPSKRLG 591
Cdd:cd05116 234 CWTYDVDERPG 244
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
343-547 6.74e-17

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 81.18  E-value: 6.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKelFAIKVLKKDVIIQdddveCTMTEKRVLALPEKPSFLVALHSCFQTMDRL 422
Cdd:cd05082   3 LNMKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCIKNDATAQ-----AFLAEASVMTQLRHSNLVQLLGVIVEEKGGL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGK--FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnifG 500
Cdd:cd05082  76 YIVTEYMAKGSLVDYLRSRGRsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKE---A 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71986426 501 DATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPF 547
Cdd:cd05082 153 SSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
354-541 7.81e-17

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 81.16  E-value: 7.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKvlkkDVIIQDDDVECT-MTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVNGG 432
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMK----ELIRFDEETQRTfLKEVKVMRCLEHPNVLKFIGVLYKD-KRLNFITEYIKGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGDATTK------ 505
Cdd:cd14221  76 TLRGIIKSMdSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLAR--LMVDEKTQpeglrs 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 71986426 506 ----------TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEML 541
Cdd:cd14221 154 lkkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
347-609 8.16e-17

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: 81.32  E-value: 8.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDD-----DVECTMtekRVLALPEKPSFLVALhscFQTMDr 421
Cdd:cd06617   2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQkrllmDLDISM---RSVDCPYTVTFYGAL---FREGD- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNGG-DLMY-QIQQVGKF-KEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCKEN 497
Cdd:cd06617  75 VWICMEVMDTSlDKFYkKVYDKGLTiPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IfgDATTKTF-CGTPDYIAPEII----LYQPYGKSVDWWAYGVLLFEMLAGQPPFD--GEDEDELFTAITEHNVSYPK-S 569
Cdd:cd06617 155 V--DSVAKTIdAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDswKTPFQQLKQVVEEPSPQLPAeK 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71986426 570 LSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFF 609
Cdd:cd06617 233 FSPEFQDFVNKCLKKNYKER--------PNYPELLQHPFF 264
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
175-260 8.43e-17

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 77.39  E-value: 8.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLI-PEDSGCKSKQKTKTLRATLNPQWNETFTYKLLPgdKDRRLSIEVWDWDRT 253
Cdd:cd04033   2 LRVKVLAGIDLAKKDIFGASDPYVKISLYdPDGNGEIDSVQTKTIKKTLNPKWNEEFFFRVNP--REHRLLFEVFDENRL 79

                ....*..
gi 71986426 254 SRNDFMG 260
Cdd:cd04033  80 TRDDFLG 86
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
39-90 8.83e-17

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 74.65  E-value: 8.83e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPG 90
Cdd:cd20803   2 HSFRKKTFHKPTYCHHCTDLLWGLLNQGYQCEVCNFVSHERCLKTVVTPCSS 53
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
351-555 8.97e-17

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 81.27  E-value: 8.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVN 430
Cdd:cd07844   5 LDKLGEGSYATVYKGRSKLTGQLVALKEIR---LEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GgDLMYQIQQVGKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifgDATTKTFCG 509
Cdd:cd07844  82 T-DLKQYMDDCGGGLSMHNVrLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAK---SVPSKTYSN 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 510 ---TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDG--EDEDEL 555
Cdd:cd07844 158 evvTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFPGstDVEDQL 209
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
345-638 9.14e-17

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 82.03  E-value: 9.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKK--DVIIQdddVECTMTEKRVLALPEKPSfLVALHSCFQT---- 418
Cdd:cd07855   4 GDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNafDVVTT---AKRTLRELKILRHFKHDN-IIAIRDILRPkvpy 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 --MDRLYFVMEFVNGgDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd07855  80 adFKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTF----CGTPDYIAPEIILYQP-YGKSVDWWAYGVLLFEMLAGQPPFDGED---------------EDELF 556
Cdd:cd07855 159 LCTSPEEHKYFmteyVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEMLGRRQLFPGKNyvhqlqliltvlgtpSQAVI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 557 TAI-----------------TEHNVSYPKSlSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFFR-RIDwfKIE 618
Cdd:cd07855 239 NAIgadrvrryiqnlpnkqpVPWETLYPKA-DQQALDLLSQMLRFDPSERI--------TVAEALQHPFLAkYHD--PDD 307
                       330       340
                ....*....|....*....|
gi 71986426 619 TRQIQPPFKPKLKTDRSTEN 638
Cdd:cd07855 308 EPDCAPPFDFDFDAEALTRE 327
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
39-88 1.06e-16

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 74.22  E-value: 1.06e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd20794   3 HLFQAKRFNRRAVCAYCSDRIWGLGRQGYKCINCKLLVHKKCHKLVKVAC 52
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
348-547 1.14e-16

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 81.64  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFlVALHSCFQTMDRLYFVME 427
Cdd:cd06635  27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNS-IEYKGCYLREHTAWLVME 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGG--DLMYQIQQVGKFKEPVAVFYAAeiAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGmcKENIFGDATtk 505
Cdd:cd06635 106 YCLGSasDLLEVHKKPLQEIEIAAITHGA--LQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG--SASIASPAN-- 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 71986426 506 TFCGTPDYIAPEIILYQPYGK---SVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd06635 180 SFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPL 224
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
354-589 1.40e-16

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: 80.17  E-value: 1.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTtkELFAIKVLKKDVIIQDddvecTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14058   1 VGRGSFGVVCKARWRN--QIVAVKIIESESEKKA-----FEVEVRQLSRVDHPN-IIKLYGACSNQKPVCLVMEYAEGGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 L---MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHS---KGIIYRDLKLDNVMLERDGH-IKITDFGM-CkenifgDATT- 504
Cdd:cd14058  73 LynvLHGKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTvLKICDFGTaC------DISTh 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 KTFC-GTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYP---KSLSKEAVSLCKA 580
Cdd:cd14058 147 MTNNkGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPpliKNCPKPIESLMTR 226

                ....*....
gi 71986426 581 LLIKNPSKR 589
Cdd:cd14058 227 CWSKDPEKR 235
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
354-541 1.51e-16

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 80.24  E-value: 1.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLkkdvIIQDDDVECT-MTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVNGG 432
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKEL----IRFDEEAQRNfLKEVKVMRSLDHPNVLKFIGVLYKD-KKLNLITEYIPGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-------KENIFGDATT 504
Cdd:cd14154  76 TLKDVLKDMARpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerLPSGNMSPSE 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 505 K-------------TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEML 541
Cdd:cd14154 156 TlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
354-544 1.53e-16

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 80.37  E-value: 1.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKvlkkDVIIQDDDVECT-MTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVNGG 432
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMK----ELIRCDEETQKTfLTEVKVMRSLDHPNVLKFIGVLYKD-KRLNLLTEFIEGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC-----------------K 495
Cdd:cd14222  76 TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekkkpppdkpttK 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 496 ENIFGDATTK---TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLaGQ 544
Cdd:cd14222 156 KRTLRKNDRKkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII-GQ 206
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
354-589 1.71e-16

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 79.62  E-value: 1.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqdDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKM----KKKEQAAHEAALLQHLQHPQ-YITLHDTYESPTSYILVLELMDDGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD---GHIKITDFGMCKEnIFGDATTKTFCGT 510
Cdd:cd14115  76 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHRHVHHLLGN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKS----LSKEAVSLCKALLIKNP 586
Cdd:cd14115 155 PEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQEDP 234

                ...
gi 71986426 587 SKR 589
Cdd:cd14115 235 RRR 237
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
342-563 2.02e-16

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 80.35  E-value: 2.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 342 VIKASDFNFLTVLGKGSFGKV---LLGEQKTTKELFAIKVLKKDvIIQDDDVECTMTEKRVLALPEKPSFL----VALHS 414
Cdd:cd05074   5 LIQEQQFTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVKMLKAD-IFSSSDIEEFLREAACMKEFDHPNVIkligVSLRS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 415 cfQTMDRL---YFVMEFVNGGDL--MYQIQQVGK--FKEPVAVF--YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH 485
Cdd:cd05074  84 --RAKGRLpipMVILPFMKHGDLhtFLLMSRIGEepFTLPLQTLvrFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 486 IKITDFGMCKENIFGDATTKTfCGTP---DYIAPEIILYQPYGKSVDWWAYGVLLFE-MLAGQPPFDGEDEDELFTAITE 561
Cdd:cd05074 162 VCVADFGLSKKIYSGDYYRQG-CASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGVENSEIYNYLIK 240

                ..
gi 71986426 562 HN 563
Cdd:cd05074 241 GN 242
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
453-549 2.23e-16

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 79.36  E-value: 2.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 453 AAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMckenifgdATTKT-FCGTPD---------YIAPEIILYQ 522
Cdd:cd14062  95 ARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGL--------ATVKTrWSGSQQfeqptgsilWMAPEVIRMQ 166
                        90       100       110
                ....*....|....*....|....*....|
gi 71986426 523 ---PYGKSVDWWAYGVLLFEMLAGQPPFDG 549
Cdd:cd14062 167 denPYSFQSDVYAFGIVLYELLTGQLPYSH 196
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
354-559 2.37e-16

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 79.60  E-value: 2.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELF--AIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCfqTMDRLYFVMEFVNG 431
Cdd:cd05115  12 LGSGNFGCVKKGVYKMRKKQIdvAIKVLKQGN--EKAVRDEMMREAQIMHQLDNPYIVRMIGVC--EAEALMLVMEMASG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIqqVGKfKEPVAVFYAAE----IAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDA--TTK 505
Cdd:cd05115  88 GPLNKFL--SGK-KDEITVSNVVElmhqVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSyyKAR 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 506 TFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAI 559
Cdd:cd05115 165 SAGKWPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFI 220
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
351-609 2.38e-16

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 80.85  E-value: 2.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKK--DVIIQdddVECTMTEKRVLALPEKPSFLVALH-----SCFQTMDRLY 423
Cdd:cd07877  22 LSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfQSIIH---AKRTYRELRLLKHMKHENVIGLLDvftpaRSLEEFNDVY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVnGGDLmYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENifgDAT 503
Cdd:cd07877  99 LVTHLM-GADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHT---DDE 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED---------------EDELFTAITEHNV-SY 566
Cdd:cd07877 174 MTGYVATRWYRAPEIMLnWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDhidqlklilrlvgtpGAELLKKISSESArNY 253
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 567 PKSLSK---------------EAVSLCKALLIKNPSKRLgctgddeSASRDIKeHPFF 609
Cdd:cd07877 254 IQSLTQmpkmnfanvfiganpLAVDLLEKMLVLDSDKRI-------TAAQALA-HAYF 303
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
174-262 2.48e-16

C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike Slp3 and Slp4/granuphilin which are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176039 [Multi-domain]  Cd Length: 125  Bit Score: 75.55  E-value: 2.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPN-GLSDPYVKCKLIPeDSGCKSKQKTKTLRATLNPQWNETFTYKL----LPGdkdRRLSIEVW 248
Cdd:cd08393  16 ELHVHVIQCQDLAAADPKkQRSDPYVKTYLLP-DKSNRGKRKTSVKKKTLNPVFNETLRYKVereeLPT---RVLNLSVW 91
                        90
                ....*....|....
gi 71986426 249 DWDRTSRNDFMGSL 262
Cdd:cd08393  92 HRDSLGRNSFLGEV 105
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
104-153 2.69e-16

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 73.11  E-value: 2.69e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20806   2 HNFKVHTFKGPHWCDYCGNFMWGLIAQGVKCEDCGFNAHKQCSKLVPHDC 51
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
104-154 2.81e-16

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 73.07  E-value: 2.81e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:cd20809   1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVCP 51
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
322-611 3.20e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 80.64  E-value: 3.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  322 PKDPAAPRASTLPLGSSNHNVIKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviiQDDDVECTMT-EKRVL 400
Cdd:PLN00034  50 PSSSSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGN---HEDTVRRQICrEIEIL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  401 ALPEKPSfLVALHSCFQTMDRLYFVMEFVNGGDLmyQIQQVGKfkEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML 480
Cdd:PLN00034 127 RDVNHPN-VVKCHDMFDHNGEIQVLLEFMDGGSL--EGTHIAD--EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  481 ERDGHIKITDFGMCKenIFgdATTKTFC----GTPDYIAPEII-------LYQPYGKsvDWWAYGVLLFEMLAGQPPFD- 548
Cdd:PLN00034 202 NSAKNVKIADFGVSR--IL--AQTMDPCnssvGTIAYMSPERIntdlnhgAYDGYAG--DIWSLGVSILEFYLGRFPFGv 275
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426  549 GEDED--ELFTAIT-EHNVSYPKSLSKEAVSLCKALLIKNPSKRLgctgddeSASRdIKEHPFFRR 611
Cdd:PLN00034 276 GRQGDwaSLMCAICmSQPPEAPATASREFRHFISCCLQREPAKRW-------SAMQ-LLQHPFILR 333
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
346-589 3.33e-16

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: 79.47  E-value: 3.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIK-VLKKDVIIqdDDVECTMTEKRVLALPEKPSfLVALHSCF----QTMd 420
Cdd:cd14049   6 NEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKkILIKKVTK--RDCMKVLREVKVLAGLQHPN-IVGYHTAWmehvQLM- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 rLYFVMEFVNGG--DLMYQIQQVGKFKEPVAVFYA-----------AEIAVGLFFLHSKGIIYRDLKLDNVMLE-RDGHI 486
Cdd:cd14049  82 -LYIQMQLCELSlwDWIVERNKRPCEEEFKSAPYTpvdvdvttkilQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 487 KITDFGMCKENIFGDA------------TTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAgqpPFDGEDED- 553
Cdd:cd14049 161 RIGDFGLACPDILQDGndsttmsrlnglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEMERa 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71986426 554 ELFTAITEHNVsyPKSLSK---EAVSLCKALLIKNPSKR 589
Cdd:cd14049 238 EVLTQLRNGQI--PKSLCKrwpVQAKYIKLLTSTEPSER 274
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
354-612 3.47e-16

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: 79.33  E-value: 3.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTkelFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14151  16 IGSGSFGTVYKGKWHGD---VAVKMLN---VTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC--KENIFGDATTKTFCGT 510
Cdd:cd14151  90 LYHHLHIIeTKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 511 PDYIAPEIILYQ---PYGKSVDWWAYGVLLFEMLAGQPPFDG-EDEDELFTAITEHNVSypKSLSKEAVSLCKALliknp 586
Cdd:cd14151 170 ILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYLS--PDLSKVRSNCPKAM----- 242
                       250       260
                ....*....|....*....|....*.
gi 71986426 587 sKRLGCtgddESASRDIKEHPFFRRI 612
Cdd:cd14151 243 -KRLMA----ECLKKKRDERPLFPQI 263
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
354-561 3.51e-16

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: 79.24  E-value: 3.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKeLFAIKVLKkdviiqdddVECTM-------TEKRVLALPEKPSFLVALHSCFQTMDRLyFVM 426
Cdd:cd14066   1 IGSGGFGTVYKGVLENGT-VVAVKRLN---------EMNCAaskkeflTELEMLGRLRHPNLVRLLGYCLESDEKL-LVY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQI-----QQVGKFKEPVAVfyAAEIAVGLFFLHSKG---IIYRDLKLDNVMLERDGHIKITDFGMCKENI 498
Cdd:cd14066  70 EYMPNGSLEDRLhchkgSPPLPWPQRLKI--AKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIP 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 499 FGDATTKT--FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14066 148 PSESVSKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVE 212
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
346-589 3.55e-16

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 79.30  E-value: 3.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 346 SDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHScFQTMDRLYFV 425
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDS-FIEDNELNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGGDLMYQIQQVGKFK----EPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIFGD 501
Cdd:cd08228  81 LELADAGDLSQMIKYFKKQKrlipERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR--FFSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 502 ATTK--TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGeDEDELFTAI------------TEHnvsYP 567
Cdd:cd08228 159 KTTAahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLFSLCqkieqcdypplpTEH---YS 234
                       250       260
                ....*....|....*....|..
gi 71986426 568 KSLsKEAVSLCkalLIKNPSKR 589
Cdd:cd08228 235 EKL-RELVSMC---IYPDPDQR 252
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
420-594 4.64e-16

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 78.38  E-value: 4.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 DRLYFVMEfVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGM---CKE 496
Cdd:cd14024  58 DRAYAFFS-RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLedsCPL 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIFGDATTKTFcGTPDYIAPEII--LYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSKEA 574
Cdd:cd14024 137 NGDDDSLTDKH-GCPAYVGPEILssRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGA 215
                       170       180
                ....*....|....*....|
gi 71986426 575 VSLCKALLIKNPSKRLGCTG 594
Cdd:cd14024 216 RCLVSCMLRRSPAERLKASE 235
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
356-547 4.73e-16

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: 78.51  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 356 KGSFGKVLLGEQKTTKELFAIKVLKKDVIiQDDDVE---CTMTEKrvlalpekpsfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd13995  14 RGAFGKVYLAQDTKTKKRMACKLIPVEQF-KPSDVEiqaCFRHEN-----------IAELYGALLWEETVHLFMEAGEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIkITDFGMC---KENIFgdaTTKTFCG 509
Cdd:cd13995  82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSvqmTEDVY---VPKDLRG 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 71986426 510 TPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd13995 158 TEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPW 195
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
174-265 5.10e-16

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 74.93  E-value: 5.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKSKqKTKTLRATLNPQWNETFTYKlLPGDKDRRLSIE--VWDWD 251
Cdd:cd00276  15 RLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKLKKK-KTSVKKGTLNPVFNEAFSFD-VPAEQLEEVSLVitVVDKD 92
                        90
                ....*....|....
gi 71986426 252 RTSRNDFMGSLSFG 265
Cdd:cd00276  93 SVGRNEVIGQVVLG 106
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
351-547 5.88e-16

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 78.52  E-value: 5.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTkelFAIKVLKkdvIIQ--DDDVECTMTEKRVLALPEKPSFLvaLHSCFQTMDRLYFVMEF 428
Cdd:cd14150   5 LKRIGTGSFGTVFRGKWHGD---VAVKILK---VTEptPEQLQAFKNEMQVLRKTRHVNIL--LFMGFMTRPNFAIITQW 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDLMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC--KENIFGDATTK 505
Cdd:cd14150  77 CEGSSLYRHLHVTeTRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQVE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 71986426 506 TFCGTPDYIAPEIILYQ---PYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd14150 157 QPSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPY 201
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
104-153 6.29e-16

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 72.12  E-value: 6.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 71986426    104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLRCSECKVKCHKKCADKVPKAC 50
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
39-88 6.51e-16

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 72.30  E-value: 6.51e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd20838   3 HRFSVHNYKRPTFCDHCGSLLYGLYKQGLQCKVCKMNVHKRCQKNVANNC 52
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
343-590 7.50e-16

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 78.15  E-value: 7.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGeqkttkelfaikvLKKDVIIQDDDVEC---------TMTEKRVLaLPE-------KP 406
Cdd:cd05032   3 LPREKITLIRELGQGSFGMVYEG-------------LAKGVVKGEPETRVaiktvnenaSMRERIEF-LNEasvmkefNC 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 407 SFLVALHSCFQTMDRLYFVMEFVNGGDL-------MYQIQQVGKFKEPVAV-FY--AAEIAVGLFFLHSKGIIYRDLKLD 476
Cdd:cd05032  69 HHVVRLLGVVSTGQPTLVVMELMAKGDLksylrsrRPEAENNPGLGPPTLQkFIqmAAEIADGMAYLAAKKFVHRDLAAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 477 NVMLERDGHIKITDFGMCKENIFGDATTKTFCGT-P-DYIAPEIILYQPYGKSVDWWAYGVLLFEM--LAGQpPFDGEDE 552
Cdd:cd05032 149 NCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLlPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMatLAEQ-PYQGLSN 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71986426 553 DELFTAITEHNV-SYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05032 228 EEVLKFVIDGGHlDLPENCPDKLLELMRMCWQYNPKMRP 266
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
453-543 7.72e-16

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 77.92  E-value: 7.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 453 AAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFgdaTTKTFCGTPDYIAPEiILYQPYGKSVDWWA 532
Cdd:cd13975 108 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAM---MSGSIVGTPIHMAPE-LFSGKYDNSVDVYA 183
                        90
                ....*....|.
gi 71986426 533 YGVLLFEMLAG 543
Cdd:cd13975 184 FGILFWYLCAG 194
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
425-589 8.38e-16

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: 77.93  E-value: 8.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDLMYQIQQVgkfKEPVAV--FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG-- 500
Cdd:cd14027  69 VMEYMEKGNLMHVLKKV---SVPLSVkgRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSkl 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 501 -----------DATTKTFCGTPDYIAPE---IILYQPYGKSvDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITEHN-- 563
Cdd:cd14027 146 tkeehneqrevDGTAKKNAGTLYYMAPEhlnDVNAKPTEKS-DVYSFAIVLWAIFANKEPYeNAINEDQIIMCIKSGNrp 224
                       170       180
                ....*....|....*....|....*...
gi 71986426 564 --VSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd14027 225 dvDDITEYCPREIIDLMKLCWEANPEAR 252
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
354-555 9.30e-16

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: 78.00  E-value: 9.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELfAIKVLKKDVIiqddDVECTMTEKRVLALPEKPSfLVALHSCFqTMDRLYFVMEFVNGGD 433
Cdd:cd05067  15 LGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM----SPDAFLAEANLMKQLQHQR-LVRLYAVV-TQEPIYIITEYMENGS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVAVF--YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05067  88 LVDFLKTPSGIKLTINKLldMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFP 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 71986426 512 -DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDEL 555
Cdd:cd05067 168 iKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEV 213
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
348-547 1.02e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 78.53  E-value: 1.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRLYFVME 427
Cdd:cd06634  17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPN-TIEYRGCYLREHTAWLVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGG--DLMYQIQQVGKFKEPVAVFYAAeiAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGmcKENIFGDATtk 505
Cdd:cd06634  96 YCLGSasDLLEVHKKPLQEVEIAAITHGA--LQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG--SASIMAPAN-- 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 71986426 506 TFCGTPDYIAPEIILYQPYGK---SVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd06634 170 SFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPL 214
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
343-589 1.05e-15

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 78.23  E-value: 1.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTT------KELFAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCF 416
Cdd:cd05053   9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLdnkpneVVTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIGKHKNIINLLGAC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDRLYFVMEFVNGGDL----------------MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML 480
Cdd:cd05053  87 TQDGPLYVVVEYASKGNLreflrarrppgeeaspDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 481 ERDGHIKITDFGMCKENIFGDATTKTFCG-TP-DYIAPEIILYQPYGKSVDWWAYGVLLFE-MLAGQPPFDGEDEDELFT 557
Cdd:cd05053 167 TEDNVMKIADFGLARDIHHIDYYRKTTNGrLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEiFTLGGSPYPGIPVEELFK 246
                       250       260       270
                ....*....|....*....|....*....|...
gi 71986426 558 AITE-HNVSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05053 247 LLKEgHRMEKPQNCTQELYMLMRDCWHEVPSQR 279
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
354-561 1.13e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 78.90  E-value: 1.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDdvecTMTEKRVLAL-----PEKPSFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd14226  21 IGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELmnkhdTENKYYIVRLKRHFMFRNHLCLVFEL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 V--NGGDLMYQ-------IQQVGKFkepvavfyAAEIAVGLFFLHSK--GIIYRDLKLDNVML--ERDGHIKITDFG-MC 494
Cdd:cd14226  97 LsyNLYDLLRNtnfrgvsLNLTRKF--------AQQLCTALLFLSTPelSIIHCDLKPENILLcnPKRSAIKIIDFGsSC 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 495 KEN--IFgdattktfcgtpDYI------APEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14226 169 QLGqrIY------------QYIqsrfyrSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 231
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
354-561 1.17e-15

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 77.92  E-value: 1.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKelFAIKVLKKDVIIQDDDVECTM-TEKRVLALPEKPSfLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd14158  23 LGEGGFGVVFKGYINDKN--VAVKKLAAMVDISTEDLTKQFeQEIQVMAKCQHEN-LVELLGYSCDGPQLCLVYTYMPNG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQVGKfKEPVAVFYAAEIAVG----LFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT--TKT 506
Cdd:cd14158 100 SLLDRLACLND-TPPLSWHMRCKIAQGtangINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTimTER 178
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 507 FCGTPDYIAPEIILYQPYGKSvDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14158 179 IVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPVDENRDPQLLLDIKE 232
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
39-88 1.23e-15

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 71.39  E-value: 1.23e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd00029   1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
353-556 1.40e-15

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR 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: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 77.92  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVL----LGEQKT-TKELFAIKVLKKDViiQDDDVECTMTEKRVLA-LPEKPSFLVALHSCFQTMDRLYFVM 426
Cdd:cd05054  14 PLGRGAFGKVIqasaFGIDKSaTCRTVAVKMLKEGA--TASEHKALMTELKILIhIGHHLNVVNLLGACTKPGGPLMVIV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDL---------------------MYQIQQV-GKFKEPVA----VFYAAEIAVGLFFLHSKGIIYRDLKLDNVML 480
Cdd:cd05054  92 EFCKFGNLsnylrskreefvpyrdkgardVEEEEDDdELYKEPLTledlICYSFQVARGMEFLASRKCIHRDLAARNILL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 481 ERDGHIKITDFGMCKEnIFGDattktfcgtPDYI------------APEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPF 547
Cdd:cd05054 172 SENNVVKICDFGLARD-IYKD---------PDYVrkgdarlplkwmAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPY 241

                ....*....
gi 71986426 548 DGEDEDELF 556
Cdd:cd05054 242 PGVQMDEEF 250
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
354-551 1.48e-15

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 77.17  E-value: 1.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDViiqddDVECTMTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVNGG- 432
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV-----DQHKIVREISLLQKLSHPNIVRYLGICVKD-EKLHPILEYVSGGc 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 --DLMYQIQQVGKFKEPVAVfyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIK---ITDFGMCKEniFGDATTK-- 505
Cdd:cd14156  75 leELLAREELPLSWREKVEL--ACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLARE--VGEMPANdp 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 506 ----TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLaGQPPFDGED 551
Cdd:cd14156 151 erklSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIPADPEV 199
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
354-609 1.52e-15

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: 77.47  E-value: 1.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKvlkkDVIIQDDDVECTMTEKRVLALPE--KPSFLVALHSCFQTMDRLYFVMEFVNG 431
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALK----RVRLDDDDEGVPSSALREICLLKelKHKNIVRLYDVLHSDKKLTLVFEYCDQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEniFGdATTKTFCG-- 509
Cdd:cd07839  84 DLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA--FG-IPVRCYSAev 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 510 -TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEML-AGQPPFDGED-EDEL------FTAITEHN-------------VSY 566
Cdd:cd07839 161 vTLWYRPPDVLFgAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDvDDQLkrifrlLGTPTEESwpgvsklpdykpyPMY 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 567 PKSLSKEAV---------SLCKALLIKNPSKRLgctgddeSASRDIKeHPFF 609
Cdd:cd07839 241 PATTSLVNVvpklnstgrDLLQNLLVCNPVQRI-------SAEEALQ-HPYF 284
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
354-549 1.56e-15

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: 76.94  E-value: 1.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE-QKTTKelFAIKVLKKDVIIQDDDVECTMTEKRVlalpeKPSFLVALHSCFQTMDRLYFVMEFVNGG 432
Cdd:cd05034   3 LGAGQFGEVWMGVwNGTTK--VAVKTLKPGTMSPEAFLQEAQIMKKL-----RHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQ--QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVmLERDGHI-KITDFG---MCKENIFGDATTKT 506
Cdd:cd05034  76 SLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNI-LVGENNVcKVADFGlarLIEDDEYTAREGAK 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 71986426 507 FcgtP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05034 155 F---PiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPG 196
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
342-568 1.83e-15

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 77.76  E-value: 1.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 342 VIKASDFNFLTVLGKGSFGKVLLG----EQKTTKELFAIKVLKKDVIIQDDdvECTMTEKRVLALPEKPSFLVALHSCF- 416
Cdd:cd05108   3 ILKETEFKKIKVLGSGAFGTVYKGlwipEGEKVKIPVAIKELREATSPKAN--KEILDEAYVMASVDNPHVCRLLGICLt 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 417 QTMDRLYFVMEFvnGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKe 496
Cdd:cd05108  81 STVQLITQLMPF--GCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAK- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 497 nIFGdATTKTFCG----TP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELfTAITEHNVSYPK 568
Cdd:cd05108 158 -LLG-AEEKEYHAeggkVPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEI-SSILEKGERLPQ 232
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
351-561 1.87e-15

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 78.21  E-value: 1.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVL--KKDVIIQdddvecTMTEKRVL-ALPEKPSflVALHSCFQTMDRLYFVME 427
Cdd:cd14225  48 LEVIGKGSFGQVVKALDHKTNEHVAIKIIrnKKRFHHQ------ALVEVKILdALRRKDR--DNSHNVIHMKEYFYFRNH 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLM----YQIQQVGKFKE-PVAVF--YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH--IKITDFGM-CKEn 497
Cdd:cd14225 120 LCITFELLgmnlYELIKKNNFQGfSLSLIrrFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSsCYE- 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426 498 ifgDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14225 199 ---HQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIME 259
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
162-269 2.34e-15

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 72.67  E-value: 2.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 162 GRLRIEAH--IENDQLTIKILEAKNLIPMDPN-GLSDPYVKCKLIPEDsgcKSKQKTKTLRATLNPQWNETFTYKLLPGD 238
Cdd:cd08390   1 GRLWFSVQydLEEEQLTVSLIKARNLPPRTKDvAHCDPFVKVCLLPDE---RRSLQSKVKRKTQNPNFDETFVFQVSFKE 77
                        90       100       110
                ....*....|....*....|....*....|..
gi 71986426 239 KDRR-LSIEVWDWDRTSRNDFMGSLSFGISEL 269
Cdd:cd08390  78 LQRRtLRLSVYDVDRFSRHCIIGHVLFPLKDL 109
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
345-561 2.41e-15

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 78.25  E-value: 2.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEctmtEKRVLALPEK-------------PSFLVA 411
Cdd:cd14224  64 AYRYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAE----EIRILEHLKKqdkdntmnvihmlESFTFR 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 412 LHSCfqtmdrLYFVMEFVNggdlMYQIQQVGKFKE---PVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH--I 486
Cdd:cd14224 140 NHIC------MTFELLSMN----LYELIKKNKFQGfslQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgI 209
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 487 KITDFGmckENIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14224 210 KVIDFG---SSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIE 281
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
351-561 2.65e-15

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 77.84  E-value: 2.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDviIQDddvecTMTEKR-----VLALPEKPSFLVALHSCF------QTM 419
Cdd:cd07850   5 LKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRP--FQN-----VTHAKRayrelVLMKLVNHKNIIGLLNVFtpqkslEEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 DRLYFVMEFVNGGdlMYQIQQVGKFKEPVAvFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKenIF 499
Cdd:cd07850  78 QDVYLVMELMDAN--LCQVIQMDLDHERMS-YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TA 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986426 500 GDATTKT-FCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd07850 153 GTSFMMTpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIE 215
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
39-90 2.73e-15

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 70.48  E-value: 2.73e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPG 90
Cdd:cd20832   2 HQFVLQHYYQVTFCNHCSGLLWGIGYQGYQCSDCEFNIHKQCIEVIEESCPG 53
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
343-549 2.78e-15

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 76.29  E-value: 2.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELfAIKVLKKDVIiqddDVECTMTEKRVLALPEKPSfLVALHSCFQTMDRL 422
Cdd:cd05068   5 IDRKSLKLLRKLGSGQFGEVWEGLWNNTTPV-AVKTLKPGTM----DPEDFLREAQIMKKLRHPK-LIQLYAVCTLEEPI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGGDLMYQIQQVGK-FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK----EN 497
Cdd:cd05068  79 YIITELMKHGSLLEYLQGKGRsLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARvikvED 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 498 IFgdaTTKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05068 159 EY---EAREGAKFPiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPG 209
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
342-549 2.83e-15

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 77.03  E-value: 2.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 342 VIKASDFNFLTVLGKGSFGKVLLG----EQKTTKELFAIKVLKkDVIIQDDDVEcTMTEKRVLALPEKPSFLVALHSCFQ 417
Cdd:cd05110   3 ILKETELKRVKVLGSGAFGTVYKGiwvpEGETVKIPVAIKILN-ETTGPKANVE-FMDEALIMASMDHPHLVRLLGVCLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 TMDRLyfVMEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKE 496
Cdd:cd05110  81 PTIQL--VTQLMPHGCLLdYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 497 nIFGDATTKTFCGTP---DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDG 549
Cdd:cd05110 159 -LEGDEKEYNADGGKmpiKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDG 214
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
104-153 2.84e-15

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 70.24  E-value: 2.84e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd00029   1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
175-281 2.99e-15

C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 73.18  E-value: 2.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLiPMDPNGLSDPYVKCKLIPEDSGckSKQKTKTLRATLNPQWNETFTYKLLPG-DKDRR----------- 242
Cdd:cd08675   1 LSVRVLECRDL-ALKSNGTCDPFARVTLNYSSKT--DTKRTKVKKKTNNPRFDEAFYFELTIGfSYEKKsfkveeedlek 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71986426 243 --LSIEVWDWDRTSRNDFMGSLSFGISELMKEAA-SGWYKLL 281
Cdd:cd08675  78 seLRVELWHASMVSGDDFLGEVRIPLQGLQQAGShQAWYFLQ 119
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
351-609 3.18e-15

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: 76.80  E-value: 3.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKvlKKDVIIQDDDVECT-MTEKRVLALPEKPSFLVALHSCFQTMDR----LYFV 425
Cdd:cd07837   6 LEKIGEGTYGKVYKARDKNTGKLVALK--KTRLEMEEEGVPSTaLREVSLLQMLSQSIYIVRLLDVEHVEENgkplLYLV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 426 MEFVNGgDLMYQIQQVGK-----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD-GHIKITDFGMckenif 499
Cdd:cd07837  84 FEYLDT-DLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGL------ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 500 GDATT---KTFCG---TPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI-------TEH--- 562
Cdd:cd07837 157 GRAFTipiKSYTHeivTLWYRAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIfrllgtpNEEvwp 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 563 NVS-------YPK-----------SLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd07837 237 GVSklrdwheYPQwkpqdlsravpDLEPEGVDLLTKMLAYDPAKRI--------SAKAALQHPYF 293
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
342-616 3.39e-15

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: 76.64  E-value: 3.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 342 VIKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKD-------VIIQDDDVectmtekrVLALPEKPsFLVALHS 414
Cdd:cd06618  11 KADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSgnkeenkRILMDLDV--------VLKSHDCP-YIVKCYG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 415 CFQTMDRLYFVMEFVNG--GDLMYQIQQvgkfkePVAVFYAAEIAV----GLFFLHSK-GIIYRDLKLDNVMLERDGHIK 487
Cdd:cd06618  82 YFITDSDVFICMELMSTclDKLLKRIQG------PIPEDILGKMTVsivkALHYLKEKhGVIHRDVKPSNILLDESGNVK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 488 ITDFGMCKENIFGDATTKTfCGTPDYIAPEIILYQPYGK---SVDWWAYGVLLFEMLAGQPPFDGEDED-ELFTAITEHN 563
Cdd:cd06618 156 LCDFGISGRLVDSKAKTRS-AGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNEE 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426 564 ---VSYPKSLSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFFRRID--------WFK 616
Cdd:cd06618 235 ppsLPPNEGFSPDFCSFVDLCLTKDHRYR--------PKYRELLQHPFIRRYEtaevdvasWFQ 290
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
354-589 3.70e-15

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: 75.84  E-value: 3.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKT---TKELFAIKVLKKDVIIQDDDVEctmtekrvlalpekpSFLV---ALHScfqtMD-----RL 422
Cdd:cd05040   3 LGDGSFGVVRRGEWTTpsgKVIQVAVKCLKSDVLSQPNAMD---------------DFLKevnAMHS----LDhpnliRL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 Y---------FVMEFVNGGDLMYQIQQV-GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG 492
Cdd:cd05040  64 YgvvlssplmMVTELAPLGSLLDRLRKDqGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 493 MCKE-NIFGDATTKTF--------CgtpdyiAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITEH 562
Cdd:cd05040 144 LMRAlPQNEDHYVMQEhrkvpfawC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKE 217
                       250       260
                ....*....|....*....|....*....
gi 71986426 563 N--VSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05040 218 GerLERPDDCPQDIYNVMLQCWAHKPADR 246
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
453-572 3.92e-15

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 76.16  E-value: 3.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 453 AAEIAVGLFFLHSKGIIYRDLKLDNVM---LERDGHI--KITDFGMCKENIFGDATTKTfcGTPDYIAPEIILYQPYGKS 527
Cdd:cd14067 120 AYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHIniKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPRIVYDEK 197
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71986426 528 VDWWAYGVLLFEMLAGQPPfdgededelftAITEHNVSYPKSLSK 572
Cdd:cd14067 198 VDMFSYGMVLYELLSGQRP-----------SLGHHQLQIAKKLSK 231
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
354-571 4.22e-15

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 75.83  E-value: 4.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE-QKTTKelFAIKVLKKDVIiqddDVECTMTEKRVLALPEKPSfLVALHSCFqTMDRLYFVMEFVNGG 432
Cdd:cd05073  19 LGAGQFGEVWMATyNKHTK--VAVKTMKPGSM----SVEAFLAEANVMKTLQHDK-LVKLHAVV-TKEPIYIITEFMAKG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLM--YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGT 510
Cdd:cd05073  91 SLLdfLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKF 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986426 511 P-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAItEHNVSYPKSLS 571
Cdd:cd05073 171 PiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRAL-ERGYRMPRPEN 232
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
343-555 4.73e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 77.01  E-value: 4.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDV--IIQDDDVEctmtEKRVLALPEKPsFLVALHSCFQTMD 420
Cdd:cd06649   2 LKDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIkpAIRNQIIR----ELQVLHECNSP-YIVGFYGAFYSDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 RLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSK-GIIYRDLKLDNVMLERDGHIKITDFGMCKENIf 499
Cdd:cd06649  77 EISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 500 gDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDEL 555
Cdd:cd06649 156 -DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
351-561 5.42e-15

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 76.52  E-value: 5.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLK-KDVIIQDDDVECTMTEK-RVLALPEKPSFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd14212   4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKnKPAYFRQAMLEIAILTLlNTKYDPEDKHHIVRLLDHFMHHGHLCIVFEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 --VNGGDLMYQIQQVGKFKEPVAVFyAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD--GHIKITDFG-MCKENifgdAT 503
Cdd:cd14212  84 lgVNLYELLKQNQFRGLSLQLIRKF-LQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGsACFEN----YT 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71986426 504 TKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITE 561
Cdd:cd14212 159 LYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIE 216
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
610-673 7.01e-15

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 69.31  E-value: 7.01e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426    610 RRIDWFKIETRQIQPPFKPKLKTDRSTENFDHSFLKLPTKMTPPDWEVLENLKGDEFSNFSFVN 673
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGIQQEPFRGFSYVF 64
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
354-618 7.61e-15

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 75.78  E-value: 7.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKE--------------LFAIKVLKKDVI--IQDDdvecTMTEKRVLALPEKPSFLVALHSCFQ 417
Cdd:cd05097  13 LGEGQFGEVHLCEAEGLAEflgegapefdgqpvLVAVKMLRADVTktARND----FLKEIKIMSRLKNPNIIRLLGVCVS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 TmDRLYFVMEFVNGGDL-MYQIQQVGKFKEPVA-----------VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH 485
Cdd:cd05097  89 D-DPLCMITEYMENGDLnQFLSQREIESTFTHAnnipsvsianlLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 486 IKITDFGMCKENIFGD-ATTKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEM--LAGQPPFDGEDEDELFTAITE 561
Cdd:cd05097 168 IKIADFGMSRNLYSGDyYRIQGRAVLPiRWMAWESILLGKFTTASDVWAFGVTLWEMftLCKEQPYSLLSDEQVIENTGE 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71986426 562 HNVSYPKSLSKEAVSLCKALLIKnpsKRLGCTgddesaSRDIKEHPFFRRIDWFKIE 618
Cdd:cd05097 248 FFRNQGRQIYLSQTPLCPSPVFK---LMMRCW------SRDIKDRPTFNKIHHFLRE 295
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
419-611 8.70e-15

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 76.36  E-value: 8.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 419 MDRLYFVMEFVNGgDLMYQIQQvGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHI-KITDFGMCK-- 495
Cdd:cd07854  88 LNSVYIVQEYMET-DLANVLEQ-GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARiv 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 ------ENIFGDATTKTFcgtpdYIAPEIILyQP--YGKSVDWWAYGVLLFEMLAGQPPFDG------------------ 549
Cdd:cd07854 166 dphyshKGYLSEGLVTKW-----YRSPRLLL-SPnnYTKAIDMWAAGCIFAEMLTGKPLFAGaheleqmqlilesvpvvr 239
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426 550 -EDEDELFTAI---TEHNVSYPK--------SLSKEAVSLCKALLIKNPSKRLGCtgddESASRdikeHPFFRR 611
Cdd:cd07854 240 eEDRNELLNVIpsfVRNDGGEPRrplrdllpGVNPEALDFLEQILTFNPMDRLTA----EEALM----HPYMSC 305
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
400-609 8.91e-15

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 75.14  E-value: 8.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 400 LALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKG--IIYRDLKLDN 477
Cdd:cd14031  66 LQHPNIVRFYDSWESVLKGKKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDN 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 478 VMLE-RDGHIKITDFGMCkeNIFGDATTKTFCGTPDYIAPEIiLYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDEL 555
Cdd:cd14031 146 IFITgPTGSVKIGDLGLA--TLMRTSFAKSVIGTPEFMAPEM-YEEHYDESVDVYAFGMCMLEMATSEYPYsECQNAAQI 222
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 556 FTAITE--HNVSYPKSLSKEAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14031 223 YRKVTSgiKPASFNKVTDPEVKEIIEGCIRQNKSERL--------SIKDLLNHAFF 270
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
350-576 9.04e-15

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 75.02  E-value: 9.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLGEQKT--TKELFAIKVLKKDVIIQDDdvECTMTEKRVLALPEKPSFLVALHSCFQTMDRLyFVME 427
Cdd:cd05087   1 YLKEIGHGWFGKVFLGEVNSglSSTQVVVKELKASASVQDQ--MQFLEEAQPYRALQHTNLLQCLAQCAEVTPYL-LVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQV----GKFKEPVAV-FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC----KENI 498
Cdd:cd05087  78 FCPLGDLKGYLRSCraaeSMAPDPLTLqRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShckyKEDY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 499 FgdATTKTFCGTPDYIAPEII-------LYQPYGKSVDWWAYGVLLFEM--LAGQPPFDGEDEDELFTAITEHNVSYPKS 569
Cdd:cd05087 158 F--VTADQLWVPLRWIAPELVdevhgnlLVVDQTKQSNVWSLGVTIWELfeLGNQPYRHYSDRQVLTYTVREQQLKLPKP 235

                ....*..
gi 71986426 570 LSKEAVS 576
Cdd:cd05087 236 QLKLSLA 242
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
39-88 9.70e-15

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 68.46  E-value: 9.70e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd20793   1 HKFKVHTYYSPTFCDHCGSLLYGLVRQGLKCKDCGMNVHHRCKENVPHLC 50
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
368-556 1.02e-14

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 75.81  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 368 KTTKELFaikVLKKDVIIQD----DDVECTMTE---KRVLALPEKPSFLvalHSCFQTMDRLYFVMEFVNGGDLMYqiqq 440
Cdd:cd14207 104 KSKRDFF---VTNKDTSLQEelikEKKEAEPTGgkkKRLESVTSSESFA---SSGFQEDKSLSDVEEEEEDSGDFY---- 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 441 vgkfKEPVA----VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKEnIFGDattktfcgtPDYI-- 514
Cdd:cd14207 174 ----KRPLTmedlISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARD-IYKN---------PDYVrk 239
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71986426 515 ----------APEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELF 556
Cdd:cd14207 240 gdarlplkwmAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDF 292
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
297-590 1.08e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 77.00  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  297 YDEDMEKVRKKMNEnfITRDNSSSKPKDPAAPRASTLPLGSSNHNVIKASDfnfltVLGKGSFGKVLLGEQKTTKELFAI 376
Cdd:PTZ00036  24 GSGKFEMNDKKLDE--EERSHNNNAGEDEDEEKMIDNDINRSPNKSYKLGN-----IIGNGSFGVVYEAICIDTSEKVAI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  377 KVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLValhSCFQTMDRLYF---VMEFVNggdlmyqiQQVGKFKE------- 446
Cdd:PTZ00036  97 KKVLQDPQYKNRELLIMKNLNHINIIFLKDYYYT---ECFKKNEKNIFlnvVMEFIP--------QTVHKYMKhyarnnh 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  447 --PVAV--FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGH-IKITDFGMCKeNIFGDATTKTFCGTPDYIAPEIIL- 520
Cdd:PTZ00036 166 alPLFLvkLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAK-NLLAGQRSVSYICSRFYRAPELMLg 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  521 YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDE-DELFTAI------TEHNVS----------------------YPKSLS 571
Cdd:PTZ00036 245 ATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSvDQLVRIIqvlgtpTEDQLKemnpnyadikfpdvkpkdlkkvFPKGTP 324
                        330
                 ....*....|....*....
gi 71986426  572 KEAVSLCKALLIKNPSKRL 590
Cdd:PTZ00036 325 DDAINFISQFLKYEPLKRL 343
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
350-541 1.20e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 74.93  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVLLGEQK----TTKELFAIKVLKKDVIIQDDDVEctmTEKRVLAlpekpsflvALHSCFQTMDR---- 421
Cdd:cd05081   8 YISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGPDQQRDFQ---REIQILK---------ALHSDFIVKYRgvsy 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 ------LYFVMEFVNGGDLMYQIQQVGKFKEPVAVF-YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC 494
Cdd:cd05081  76 gpgrrsLRLVMEYLPSGCLRDFLQRHRARLDASRLLlYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLA 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426 495 KenIFGDATTKTFCGTPD-----YIAPEIILYQPYGKSVDWWAYGVLLFEML 541
Cdd:cd05081 156 K--LLPLDKDYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
422-609 1.25e-14

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 73.93  E-value: 1.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFvngGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKI-----TDFGMCKE 496
Cdd:cd14023  62 VFFEKDF---GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLrleslEDTHIMKG 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NifgDATTKTFCGTPDYIAPEII----LYQpyGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAITEHNVSYPKSLSK 572
Cdd:cd14023 139 E---DDALSDKHGCPAYVSPEILnttgTYS--GKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSP 213
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 71986426 573 EAVSLCKALLIKNPSKRLgctgddesASRDIKEHPFF 609
Cdd:cd14023 214 KARCLIRSLLRREPSERL--------TAPEILLHPWF 242
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
348-539 1.28e-14

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: 74.27  E-value: 1.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLK------KDVIIQDDDVECTMTekrvlaLPEKPSfLVALHSCFQTMDR 421
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRsrfrgeKDRKRKLEEVERHEK------LGEHPN-CVRFIKAWEEKGI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNGGDLMY--QIQQVGKfKEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG----MCK 495
Cdd:cd14050  76 LYIQTELCDTSLQQYceETHSLPE-SEVWNILL--DLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGlvveLDK 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 71986426 496 ENIfGDATTktfcGTPDYIAPEiILYQPYGKSVDWWAYGVLLFE 539
Cdd:cd14050 153 EDI-HDAQE----GDPRYMAPE-LLQGSFTKAADIFSLGITILE 190
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
354-589 1.43e-14

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 74.72  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVECTMTEKRVlalpeKPSFLVALHSCFqTMDRLYFVMEFVNGGD 433
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMMPEAFLQEAQIMKKL-----RHDKLVPLYAVV-SEEPIYIVTEFMGKGS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQV-GKF-KEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05069  93 LLDFLKEGdGKYlKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 -DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNVSYPKSLSKEAVSLCKALLIKNPSK 588
Cdd:cd05069 173 iKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERgYRMPCPQGCPESLHELMKLCWKKDPDE 252

                .
gi 71986426 589 R 589
Cdd:cd05069 253 R 253
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
345-590 1.65e-14

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 75.42  E-value: 1.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 345 ASDFNFLTVLGKGSFGKVLLGEQKTTKELFAIKVL----------------------KKDVIIQDDDVECTMTekrvlal 402
Cdd:cd07849   4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfehqtyclrtlreikillrfKHENIIGILDIQRPPT------- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 403 pekpsflvalhscFQTMDRLYFVMEFVNGgDLmYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER 482
Cdd:cd07849  77 -------------FESFKDVYIVQELMET-DL-YKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 483 DGHIKITDFGMCK----ENIFGDATTKtFCGTPDYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGED------ 551
Cdd:cd07849 142 NCDLKICDFGLARiadpEHDHTGFLTE-YVATRWYRAPEIMLnSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDylhqln 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986426 552 ----------EDELFTAITEHNVSYPKSL---------------SKEAVSLCKALLIKNPSKRL 590
Cdd:cd07849 221 lilgilgtpsQEDLNCIISLKARNYIKSLpfkpkvpwnklfpnaDPKALDLLDKMLTFNPHKRI 284
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
104-154 1.82e-14

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 68.27  E-value: 1.82e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:cd20797   4 HVVEVEQYMTPTFCDYCGEMLTGLMKQGVKCKNCRCNFHKRCANAPRNNCA 54
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
406-542 1.82e-14

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 73.66  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 406 PSFLVALHSCFQTmDRLYFVMEFVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERD-- 483
Cdd:cd14155  48 PNILRFMGVCVHQ-GQLHALTEYINGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDen 126
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986426 484 GHIKIT-DFGMC-KENIFGDATTK-TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLA 542
Cdd:cd14155 127 GYTAVVgDFGLAeKIPDYSDGKEKlAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIA 188
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
433-555 1.88e-14

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: 74.30  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQvgkfkepvavfyaaeiavGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCgTPD 512
Cdd:cd07862 114 DMMFQLLR------------------GLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVV-TLW 174
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71986426 513 YIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDG-EDEDEL 555
Cdd:cd07862 175 YRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGsSDVDQL 218
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
104-153 1.99e-14

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 68.54  E-value: 1.99e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20840  11 HALNVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNC 60
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
352-589 2.29e-14

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 74.23  E-value: 2.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 352 TVLGKGSFGKVLLGEQKTTKEL-----FAIKVLKKDViiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTmDRLYFVM 426
Cdd:cd05045   6 KTLGEGEFGKVVKATAFRLKGRagyttVAVKMLKENA--SSSELRDLLSEFNLLKQVNHPHVIKLYGACSQD-GPLLLIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKF--------------------KEPVAV----FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER 482
Cdd:cd05045  83 EYAKYGSLRSFLRESRKVgpsylgsdgnrnssyldnpdERALTMgdliSFAWQISRGMQYLAEMKLVHRDLAARNVLVAE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 483 DGHIKITDFGMCKENIFGDATTKTFCG-TP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAI 559
Cdd:cd05045 163 GRKMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLFNLL 242
                       250       260       270
                ....*....|....*....|....*....|.
gi 71986426 560 -TEHNVSYPKSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd05045 243 kTGYRMERPENCSEEMYNLMLTCWKQEPDKR 273
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
343-590 2.41e-14

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) 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 of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 73.85  E-value: 2.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGE-----QKTTKELFAIKVLKKDVIIQDDDVEctmTEKRVLALPEKpSFLVALHSCFQ 417
Cdd:cd05092   2 IKRRDIVLKWELGEGAFGKVFLAEchnllPEQDKMLVAVKALKEATESARQDFQ---REAELLTVLQH-QHIVRFYGVCT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 418 TMDRLYFVMEFVNGGDLMY---------------QIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLER 482
Cdd:cd05092  78 EGEPLIMVFEYMRHGDLNRflrshgpdakildggEGQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 483 DGHIKITDFGMCKEnIFGDATTKTFCGT--P-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTA 558
Cdd:cd05092 158 GLVVKIGDFGMSRD-IYSTDYYRVGGRTmlPiRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIEC 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 71986426 559 ITE-HNVSYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05092 237 ITQgRELERPRTCPPEVYAIMQGCWQREPQQRH 269
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
354-609 2.72e-14

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 73.50  E-value: 2.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTK------ELFAIKVLKKDVIIQDDDVECTmtekRVLALPEKPSFLVALHSCFQTMDRLYFVME 427
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTvevawcELQTRKLSKGERQRFSEEVEML----KGLQHPNIVRFYDSWKSTVRGHKCIILVTE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 428 FVNGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKG--IIYRDLKLDNVMLE-RDGHIKITDFGMC--KENIFgda 502
Cdd:cd14033  85 LMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLAtlKRASF--- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 503 tTKTFCGTPDYIAPEIiLYQPYGKSVDWWAYGVLLFEMLAGQPPF-DGEDEDELFTAITEHnvSYPKSLSKEAVSLCKAL 581
Cdd:cd14033 162 -AKSVIGTPEFMAPEM-YEEKYDEAVDVYAFGMCILEMATSEYPYsECQNAAQIYRKVTSG--IKPDSFYKVKVPELKEI 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 71986426 582 LiknpskrLGC--TGDDESAS-RDIKEHPFF 609
Cdd:cd14033 238 I-------EGCirTDKDERFTiQDLLEHRFF 261
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
174-284 2.73e-14

C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176055 [Multi-domain]  Cd Length: 135  Bit Score: 70.30  E-value: 2.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKSKqKTKTLRATLNPQWNETFTYKLLPGD-KDRRLSIEVWDWDR 252
Cdd:cd08410  15 RLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGLKLIKTK-KTSCMRGTIDPFYNESFSFKVPQEElENVSLVFTVYGHNV 93
                        90       100       110
                ....*....|....*....|....*....|..
gi 71986426 253 TSRNDFMGSLSFGISELMKEAASGWYKLLSAE 284
Cdd:cd08410  94 KSSNDFIGRIVIGQYSSGPSETNHWRRMLNSQ 125
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
354-594 3.04e-14

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) 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 of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 73.92  E-value: 3.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE-----QKTTKELFAIKVLKKdviiQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEF 428
Cdd:cd05093  13 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKD----ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 429 VNGGDL-------------MYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK 495
Cdd:cd05093  89 MKHGDLnkflrahgpdavlMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 EnIFGDATTKTFCGTP---DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITEHNV-SYPKSL 570
Cdd:cd05093 169 D-VYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRPRTC 247
                       250       260
                ....*....|....*....|....
gi 71986426 571 SKEAVSLCKALLIKNPSKRLGCTG 594
Cdd:cd05093 248 PKEVYDLMLGCWQREPHMRLNIKE 271
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
354-547 3.04e-14

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: 72.95  E-value: 3.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGeqKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYFVMEFVNGGD 433
Cdd:cd14064   1 IGSGSFGKVYKG--RCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTQYVSGGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQQVGKFKEPVA-VFYAAEIAVGLFFLH--SKGIIYRDLKLDNVMLERDGHIKITDFGMCK--ENIFGDATTKTfC 508
Cdd:cd14064  79 LFSLLHEQKRVIDLQSkLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRflQSLDEDNMTKQ-P 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 71986426 509 GTPDYIAPEIILY-QPYGKSVDWWAYGVLLFEMLAGQPPF 547
Cdd:cd14064 158 GNLRWMAPEVFTQcTRYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
343-590 3.11e-14

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: 73.65  E-value: 3.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 343 IKASDFNFLTVLGKGSFGKVLLGE-----QKTTKELFAIKVLKK---DVIIQDDDVECTMtekrvLALPEKPSFLVALHS 414
Cdd:cd05049   2 IKRDTIVLKRELGEGAFGKVFLGEcynlePEQDKMLVAVKTLKDassPDARKDFEREAEL-----LTNLQHENIVKFYGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 415 CFQTmDRLYFVMEFVNGGDLMYQIQQVGK-----FKEPVAVF---------YAAEIAVGLFFLHSKGIIYRDLKLDNVML 480
Cdd:cd05049  77 CTEG-DPLLMVFEYMEHGDLNKFLRSHGPdaaflASEDSAPGeltlsqllhIAVQIASGMVYLASQHFVHRDLATRNCLV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 481 ERDGHIKITDFGMCKEnIFgdattktfcgTPDY-------------IAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPP 546
Cdd:cd05049 156 GTNLVVKIGDFGMSRD-IY----------STDYyrvgghtmlpirwMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQP 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 71986426 547 FDGEDEDELFTAITEHNV-SYPKSLSKEAVSLCKALLIKNPSKRL 590
Cdd:cd05049 225 WFQLSNTEVIECITQGRLlQRPRTCPSEVYAVMLGCWKREPQQRL 269
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
104-154 3.16e-14

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 67.40  E-value: 3.16e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:cd20832   2 HQFVLQHYYQVTFCNHCSGLLWGIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
C2A_Munc13-like cd08676
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
175-280 3.28e-14

C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176058 [Multi-domain]  Cd Length: 153  Bit Score: 70.48  E-value: 3.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLIP---EDSGCKSKQK--------------------TKTLRATLNPQWNETFt 231
Cdd:cd08676  30 LKVTVIEAKGLLAKDVNGFSDPYCMLGIVPasrERNSEKSKKRkshrkkavlkdtvpaksikvTEVKPQTLNPVWNETF- 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 232 yKLLPGD-KDRRLSIEVWDWDrtsrNDFMGSLSFGISELMKEAASGWYKL 280
Cdd:cd08676 109 -RFEVEDvSNDQLHLDIWDHD----DDFLGCVNIPLKDLPSCGLDSWFKL 153
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
348-551 3.31e-14

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 74.43  E-value: 3.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAIKVLKkDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDR----LY 423
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIN-DVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRRefkdIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVnGGDLMYQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENiFGDAT 503
Cdd:cd07859  81 VVFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVA-FNDTP 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71986426 504 TKTF----CGTPDYIAPEII--LYQPYGKSVDWWAYGVLLFEMLAGQPPFDGED 551
Cdd:cd07859 159 TAIFwtdyVATRWYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFPGKN 212
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
358-610 3.67e-14

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 73.51  E-value: 3.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 358 SFGKVLLGEQKTTKELFAIKVLKKDVIiqdddvecTMTEKRvlalpeKPSFLVALHSCFQTMDRLYFVMEFVNG------ 431
Cdd:cd14011  28 VFEKKQLEEYSKRDREQILELLKRGVK--------QLTRLR------HPRILTVQHPLEESRESLAFATEPVFAslanvl 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQVGKFKEPVavFYAAEIAVGLF-------FLH-SKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDAT 503
Cdd:cd14011  94 GERDNMPSPPPELQDYK--LYDVEIKYGLLqisealsFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQ 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 504 TKTFCG-----------TPDYIAPEIILYQPYGKSVDWWAYGVLLFEML-AGQPPFDGEDE----DELFTAITEHNVSYP 567
Cdd:cd14011 172 FPYFREydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNllsyKKNSNQLRQLSLSLL 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71986426 568 KSLSKEAVSLCKALLIKNPSKRLGCTgddesasrDIKEHPFFR 610
Cdd:cd14011 252 EKVPEELRDHVKTLLNVTPEVRPDAE--------QLSKIPFFD 286
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
409-589 3.70e-14

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 73.53  E-value: 3.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 409 LVALHSCFQTMDRLYFVMEFVNGGDLMYQIQQVGKFK----EPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDG 484
Cdd:cd08229  86 VIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKrlipEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 485 HIKITDFGMCKenIFGDATTK--TFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFDGeDEDELFTAITE- 561
Cdd:cd08229 166 VVKLGDLGLGR--FFSSKTTAahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLYSLCKKi 242
                       170       180       190
                ....*....|....*....|....*....|..
gi 71986426 562 HNVSYP----KSLSKEAVSLCKALLIKNPSKR 589
Cdd:cd08229 243 EQCDYPplpsDHYSEELRQLVNMCINPDPEKR 274
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
175-297 4.05e-14

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 76.34  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  175 LTIKILEAKNLIPMDPNGLSDPYVKCKLipedsGCKSKQKTKTLRATLNPQWNETFTYKLLPGDKDrRLSIEVWDWDRTS 254
Cdd:COG5038 1042 LTIMLRSGENLPSSDENGYSDPFVKLFL-----NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKD-VLTINVNDWDSGE 1115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 71986426  255 RNDFMGSLSFGISELMKEAASGWYKLLSAEEGEFYNINITPEY 297
Cdd:COG5038 1116 KNDLLGTAEIDLSKLEPGGTTNSNIPLDGKTFIVLDGTLHPGF 1158
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
354-556 4.31e-14

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: 72.64  E-value: 4.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVECTMTEKRVlalpeKPSFLVALHSCFqTMDRLYFVMEFVNGGD 433
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTKV-AIKTLKPGTMSPEAFLEEAQIMKKL-----RHDKLVQLYAVV-SEEPIYIVTEFMSKGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LM-YQIQQVGKF-KEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd14203  76 LLdFLKDGEGKYlKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFP 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71986426 512 -DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELF 556
Cdd:cd14203 156 iKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVL 202
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
354-563 4.60e-14

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 73.12  E-value: 4.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE--QKTTKELFAIKVLKKdVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYF-----VM 426
Cdd:cd05075   8 LGEGEFGSVMEGQlnQDDSVLKVAVKTMKI-AICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESEGYpspvvIL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 427 EFVNGGDLMYQIQQVGKFKEPV------AVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG 500
Cdd:cd05075  87 PFMKHGDLHSFLLYSRLGDCPVylptqmLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIYNG 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 501 DATTK-TFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITEHN 563
Cdd:cd05075 167 DYYRQgRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQGN 232
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
104-153 5.02e-14

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 67.35  E-value: 5.02e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20839   8 HALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 57
C2B_Synaptotagmin-3-5-6-9-10 cd08403
C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a ...
174-265 5.26e-14

C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 3, a member of class 3 synaptotagmins, is located in the brain and localized to the active zone and plasma membrane. It functions as a Ca2+ sensor for fast exocytosis. It, along with synaptotagmins 5,6, and 10, has disulfide bonds at its N-terminus. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176048 [Multi-domain]  Cd Length: 134  Bit Score: 69.46  E-value: 5.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKsKQKTKTLRATLNPQWNETFTYKLLPGDKDR-RLSIEVWDWDR 252
Cdd:cd08403  15 RLTLTIIKARNLKAMDITGFSDPYVKVSLMCEGRRLK-KKKTSVKKNTLNPTYNEALVFDVPPENVDNvSLIIAVVDYDR 93
                        90
                ....*....|...
gi 71986426 253 TSRNDFMGSLSFG 265
Cdd:cd08403  94 VGHNELIGVCRVG 106
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
104-153 5.87e-14

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 67.37  E-value: 5.87e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20841  11 HTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNC 60
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
353-543 6.21e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 72.29  E-value: 6.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKttKELFAIKVLKKDViiqddDVECTMTEKRVLALPEKPSfLVALHSCfQTMDRLyFVMEFVNGG 432
Cdd:cd14068   1 LLGDGGFGSVYRAVYR--GEDVAVKIFNKHT-----SFRLLRQELVVLSHLHHPS-LVALLAA-GTAPRM-LVMELAPKG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 433 DLMYQIQQ-VGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVM---LERDGHI--KITDFGM----CKENIfgda 502
Cdd:cd14068  71 SLDALLQQdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIiaKIADYGIaqycCRMGI---- 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71986426 503 ttKTFCGTPDYIAPEIILYQ-PYGKSVDWWAYGVLLFEMLAG 543
Cdd:cd14068 147 --KTSEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTC 186
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
354-548 6.28e-14

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 73.37  E-value: 6.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKdviiQDDDVECTMTEKRVLAL-----PEKPSFLVALHSCFQ-------TMDR 421
Cdd:cd14134  20 LGEGTFGKVLECWDRKRKRYVAVKIIRN----VEKYREAAKIEIDVLETlaekdPNGKSHCVQLRDWFDyrghmciVFEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 L----Y-FVMEFVNGGDLMYQIQQVGKfkepvavfyaaEIAVGLFFLHSKGIIYRDLKLDNVMLE--------------- 481
Cdd:cd14134  96 LgpslYdFLKKNNYGPFPLEHVQHIAK-----------QLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrq 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426 482 ----RDGHIKITDFGMCkenIFGDATTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLFEMLAGQPPFD 548
Cdd:cd14134 165 irvpKSTDIKLIDFGSA---TFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQ 232
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
175-286 6.46e-14

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 68.47  E-value: 6.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPN------GLSDPYVKCKLIPEdsgcksKQKTKTLRATLNPQWNETFTYkLLPGDKDRRLSIEVW 248
Cdd:cd08391   3 LRIHVIEAQDLVAKDKFvgglvkGKSDPYVIVRVGAQ------TFKSKVIKENLNPKWNEVYEA-VVDEVPGQELEIELF 75
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71986426 249 DWDrTSRNDFMGSLSFGISELMKEAASG-WYKLLSAEEG 286
Cdd:cd08391  76 DED-PDKDDFLGRLSIDLGSVEKKGFIDeWLPLEDVKSG 113
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
350-589 6.62e-14

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR 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: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 72.90  E-value: 6.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 350 FLTVLGKGSFGKVL----LGEQKTTKEL-FAIKVLKKDViiQDDDVECTMTEKRVLA-LPEKPSFLVALHSCFQTmDRLY 423
Cdd:cd05055  39 FGKTLGAGAFGKVVeataYGLSKSDAVMkVAVKMLKPTA--HSSEREALMSELKIMShLGNHENIVNLLGACTIG-GPIL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQqvgKFKEPVAVF-----YAAEIAVGLFFLHSKGIIYRDLKLDNVMLErDGHI-KITDFGMCKEn 497
Cdd:cd05055 116 VITEYCCYGDLLNFLR---RKRESFLTLedllsFSYQVAKGMAFLASKNCIHRDLAARNVLLT-HGKIvKICDFGLARD- 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 498 IFGDAT--TKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE--HNVSYPKSLS 571
Cdd:cd05055 191 IMNDSNyvVKGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKegYRMAQPEHAP 270
                       250
                ....*....|....*...
gi 71986426 572 KEAVSLCKALLIKNPSKR 589
Cdd:cd05055 271 AEIYDIMKTCWDADPLKR 288
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
459-609 6.73e-14

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: 72.69  E-value: 6.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 459 GLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCgTPDYIAPEIILYQPYGKSVDWWAYGVLLF 538
Cdd:cd07863 120 GLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMALTPVVV-TLWYRAPEVLLQSTYATPVDMWSVGCIFA 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 539 EMLAGQPPFDGEDE-DEL---FTAIT-------EHNVSYPKS----------------LSKEAVSLCKALLIKNPSKRLg 591
Cdd:cd07863 199 EMFRRKPLFCGNSEaDQLgkiFDLIGlppeddwPRDVTLPRGafsprgprpvqsvvpeIEESGAQLLLEMLTFNPHKRI- 277
                       170
                ....*....|....*...
gi 71986426 592 ctgddeSASRDIkEHPFF 609
Cdd:cd07863 278 ------SAFRAL-QHPFF 288
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
175-260 7.19e-14

C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 68.58  E-value: 7.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSgcKSKQkTKTLRATLNPQWNETFTYKLLPGDKDRR-LSIEVWDWDRT 253
Cdd:cd08387  18 LNVKLIQARNLQPRDFSGTADPYCKVRLLPDRS--NTKQ-SKIHKKTLNPEFDESFVFEVPPQELPKRtLEVLLYDFDQF 94

                ....*..
gi 71986426 254 SRNDFMG 260
Cdd:cd08387  95 SRDECIG 101
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
348-589 7.42e-14

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 72.33  E-value: 7.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKTTKELFAikvLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTMDR----LY 423
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYA---LKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEAGgkkeVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 424 FVMEFVNGGDLMYQIQQVGK----FKEPVAVFYAAEIAVGLFFLHS---KGIIYRDLKLDNVMLERDGHIKITDFG-MCK 495
Cdd:cd13986  79 LLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPILMDLGsMNP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 496 ENIFGDATTK--------TFCGTPDYIAPEIILYQPYG---KSVDWWAYGVLLFEMLAGQPPFDGEDE--DELFTAITEH 562
Cdd:cd13986 159 ARIEIEGRREalalqdwaAEHCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFERIFQkgDSLALAVLSG 238
                       250       260
                ....*....|....*....|....*....
gi 71986426 563 NVSYPK--SLSKEAVSLCKALLIKNPSKR 589
Cdd:cd13986 239 NYSFPDnsRYSEELHQLVKSMLVVNPAER 267
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
354-568 7.86e-14

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 72.24  E-value: 7.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGE--QKTTKELFAIKVLKKDVIIQDDDVecTMTEKRVLALPEKPSFLVALHSCFQTMDRLyFVMEFVNG 431
Cdd:cd05042   3 IGNGWFGKVLLGEiySGTSVAQVVVKELKASANPKEQDT--FLKEGQPYRILQHPNILQCLGQCVEAIPYL-LVMEFCDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDL--MYQIQQVGKFKEPVAVF---YAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMC----KENIFGDA 502
Cdd:cd05042  80 GDLkaYLRSEREHERGDSDTRTlqrMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhsryKEDYIETD 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71986426 503 TTKTFcgtP-DYIAPEII-------LYQPYGKSVDWWAYGVLLFEM--LAGQPPFDGEDEDELFTAITEHNVSYPK 568
Cdd:cd05042 160 DKLWF---PlRWTAPELVtefhdrlLVVDQTKYSNIWSLGVTLWELfeNGAQPYSNLSDLDVLAQVVREQDTKLPK 232
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
347-589 8.06e-14

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: 72.00  E-value: 8.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 347 DFNFLTVLGKGSFGKVLLGEQKTTkelFAIKVLKKDVIIQDDDV---ECTMTEKRV----LALpekpsFLVAlhscfqTM 419
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRGRWHGD---VAIKLLNIDYLNEEQLEafkEEVAAYKNTrhdnLVL-----FMGA------CM 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 420 D--RLYFVMEFVNGGDLMYQI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLErDGHIKITDFGMCKE 496
Cdd:cd14063  67 DppHLAIVTSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGLFSL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 497 NIF-----GDATTKTFCGTPDYIAPEII----------LYQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTAI-- 559
Cdd:cd14063 146 SGLlqpgrREDTLVIPNGWLCYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVgc 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 71986426 560 ----TEHNVSYPKSLsKEAVSLCKALlikNPSKR 589
Cdd:cd14063 226 gkkqSLSQLDIGREV-KDILMQCWAY---DPEKR 255
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
104-153 9.28e-14

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 66.16  E-value: 9.28e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20796   2 HTFVVHTYTKPTVCQHCKKLLKGLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
104-153 9.78e-14

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 65.90  E-value: 9.78e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20827   2 HRFEKHNFTTPTYCDYCSSLLWGLVKTGMRCADCGYSCHEKCLEHVPKNC 51
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
174-261 9.85e-14

C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fourth C2 repeat, C2D, and has a type-II topology.


Pssm-ID: 175984 [Multi-domain]  Cd Length: 135  Bit Score: 68.72  E-value: 9.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 174 QLTIKILEAKNLIPMDPNGLSDPYVKCKLipedsGCKSkQKTKTLRATLNPQWNETFTYK--LLPGDKD--RR----LSI 245
Cdd:cd04017   2 QLRAYIYQARDLLAADKSGLSDPFARVSF-----LNQS-QETEVIKETLSPTWDQTLIFDevELYGSPEeiAQnpplVVV 75
                        90
                ....*....|....*.
gi 71986426 246 EVWDWDRTSRNDFMGS 261
Cdd:cd04017  76 ELFDQDSVGKDEFLGR 91
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
354-492 1.14e-13

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: 68.62  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKkdvIIQDDDVECTMTEKRVLALPEKPSFLVA--LHSCfQTMDRLYFVMEFVNG 431
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGD---DVNNEEGEDLESEMDILRRLKGLELNIPkvLVTE-DVDGPNILLMELVKG 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986426 432 GDLMYQIQQVGKF-KEPVAVFYaaEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG 492
Cdd:cd13968  77 GTLIAYTQEEELDeKDVESIMY--QLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
351-560 1.43e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 72.02  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIK--------------VLKKDVIIQ---DDDVECTMTEKRVLALPE---KPSFlv 410
Cdd:cd07865  17 LAKIGQGTFGEVFKARHRKTGQIVALKkvlmenekegfpitALREIKILQllkHENVVNLIEICRTKATPYnryKGSI-- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 411 alhscfqtmdrlYFVMEFVNGgDLMYQIQQVG-KFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKIT 489
Cdd:cd07865  95 ------------YLVFEFCEH-DLAGLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 490 DFGMCKenifgdATTKTFCGTPD----------YIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDEDELFTA 558
Cdd:cd07865 162 DFGLAR------AFSLAKNSQPNrytnrvvtlwYRPPELLLgERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTL 235

                ..
gi 71986426 559 IT 560
Cdd:cd07865 236 IS 237
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
102-154 1.58e-13

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 65.54  E-value: 1.58e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71986426 102 QQHKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:cd20828   4 QPHNFEPHSFVTPTNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
353-590 1.65e-13

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: 71.39  E-value: 1.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKTTKELFAIKVL------KKDVIIQDddvECTMteKRVLALPEKPSFL----VALHSCFQTMDRL 422
Cdd:cd14036   7 VIAEGGFAFVYEAQDVGTGKEYALKRLlsneeeKNKAIIQE---INFM--KKLSGHPNIVQFCsaasIGKEESDQGQAEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 423 YFVMEFVNGG--DLMYQIQQVGKFK--EPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFG------ 492
Cdd:cd14036  82 LLLTELCKGQlvDFVKKVEAPGPFSpdTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQIKLCDFGsattea 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 493 -------------MCKENIfgdaTTKTfcgTPDYIAPEII-LYQ--PYGKSVDWWAYGVLLFEMLAGQPPFdgEDEDELf 556
Cdd:cd14036 162 hypdyswsaqkrsLVEDEI----TRNT---TPMYRTPEMIdLYSnyPIGEKQDIWALGCILYLLCFRKHPF--EDGAKL- 231
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71986426 557 tAITEHNVSYPKSLSKEAV--SLCKALLIKNPSKRL 590
Cdd:cd14036 232 -RIINAKYTIPPNDTQYTVfhDLIRSTLKVNPEERL 266
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
353-556 1.87e-13

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 71.03  E-value: 1.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVL---LGEQKTTKELFAIKVLKKDVIIQDDdVECTMTEKRVLALPEKPSFLVALHSCFQTMDRLYF----- 424
Cdd:cd05035   6 ILGEGEFGSVMeaqLKQDDGSQLKVAVKTMKVDIHTYSE-IEEFLSEAACMKDFDHPNVMRLIGVCFTASDLNKPpspmv 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 425 VMEFVNGGDL----MYQIQQVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENI 498
Cdd:cd05035  85 ILPFMKHGDLhsylLYSRLGGLPEKLPLQtlLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIY 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986426 499 FGDATTKT-FCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELF 556
Cdd:cd05035 165 SGDYYRQGrISKMPvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIY 225
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
354-559 2.20e-13

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 70.87  E-value: 2.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELfAIKVLKKDVIIQDDDVECTMTEKRVlalpeKPSFLVALHSCFqTMDRLYFVMEFVNGGD 433
Cdd:cd05070  17 LGNGQFGEVWMGTWNGNTKV-AIKTLKPGTMSPESFLEEAQIMKKL-----KHDKLVQLYAVV-SEEPIYIVTEYMSKGS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 434 LMYQIQ--QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTFCGTP 511
Cdd:cd05070  90 LLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFP 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 512 -DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAI 559
Cdd:cd05070 170 iKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 219
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
354-547 2.25e-13

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 71.75  E-value: 2.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVEctMTEKRVLALPEKPSF--LVALHSCFQTMDRLyFVMEFVNG 431
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQ--MREFEVLKKLNHKNIvkLFAIEEELTTRHKV-LVMELCPC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 432 GDLMYQIQQ-VGKFKEPVAVFYAA--EIAVGLFFLHSKGIIYRDLKLDNVM--LERDGH--IKITDFGMCKEnIFGDATT 504
Cdd:cd13988  78 GSLYTVLEEpSNAYGLPESEFLIVlrDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARE-LEDDEQF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 505 KTFCGTPDYIAPEI----ILYQPYGKS----VDWWAYGVLLFEMLAGQPPF 547
Cdd:cd13988 157 VSLYGTEEYLHPDMyeraVLRKDHQKKygatVDLWSIGVTFYHAATGSLPF 207
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
104-151 2.65e-13

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 64.66  E-value: 2.65e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPN 151
Cdd:cd20817   1 HSFQEHTFKKPTFCDVCKELLVGLSKQGLRCKNCKMNVHHKCQEGVPD 48
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
351-548 2.77e-13

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 70.72  E-value: 2.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 351 LTVLGKGSFGKVLLGEQKTTKELFAIKVLKKDVIIQDDDVECTMTEKRVLALPEKPSFLVALHSCFQTmDRLYFVMEFVN 430
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEP-EFLGIVTEYMT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 431 GGDLMYQIQQVGKFKE---PVAVFYAAEIAVGLFFLH--SKGIIYRDLKLDNVMLERDGHIKITDFGMCKENIFG----- 500
Cdd:cd14026  81 NGSLNELLHEKDIYPDvawPLRLRILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSisqsr 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71986426 501 DATTKTFCGTPDYIAPEIilYQPYGKS-----VDWWAYGVLLFEMLAGQPPFD 548
Cdd:cd14026 161 SSKSAPEGGTIIYMPPEE--YEPSQKRrasvkHDIYSYAIIMWEVLSRKIPFE 211
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
353-589 2.88e-13

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) 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. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 70.45  E-value: 2.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 353 VLGKGSFGKVLLGEQKT--TKELFAIKVLKKdvIIQDDDVECTMTEKRVLA-LPEKPSFLVALHSCfQTMDRLYFVMEFV 429
Cdd:cd05047   2 VIGEGNFGQVLKARIKKdgLRMDAAIKRMKE--YASKDDHRDFAGELEVLCkLGHHPNIINLLGAC-EHRGYLYLAIEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 430 NGGDLMYQIQQVGKFKEPVA----------------VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGM 493
Cdd:cd05047  79 PHGNLLDFLRKSRVLETDPAfaianstastlssqqlLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 494 CK-ENIFgdaTTKTFCGTP-DYIAPEIILYQPYGKSVDWWAYGVLLFEMLA-GQPPFDGEDEDELFTAITE-HNVSYPKS 569
Cdd:cd05047 159 SRgQEVY---VKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQgYRLEKPLN 235
                       250       260
                ....*....|....*....|
gi 71986426 570 LSKEAVSLCKALLIKNPSKR 589
Cdd:cd05047 236 CDDEVYDLMRQCWREKPYER 255
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
354-541 2.91e-13

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: 70.73  E-value: 2.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 354 LGKGSFGKVLL----GEQKTTKELFAIKVLKKDViiqdddvectmTEKRVLALPEKPSFLVALHS---------CFQTMD 420
Cdd:cd05079  12 LGEGHFGKVELcrydPEGDNTGEQVAVKSLKPES-----------GGNHIADLKKEIEILRNLYHenivkykgiCTEDGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 421 R-LYFVMEFVNGGDLM-YQIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLERDGHIKITDFGMCK--E 496
Cdd:cd05079  81 NgIKLIMEFLPSGSLKeYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKaiE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 71986426 497 NIFGDATTKTFCGTPDY-IAPEIILYQPYGKSVDWWAYGVLLFEML 541
Cdd:cd05079 161 TDKEYYTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
39-88 2.98e-13

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 64.38  E-value: 2.98e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd20837   1 HRFKVYNYMSPTFCDHCGSLLWGLFRQGLKCEECGMNVHHKCQKKVANLC 50
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
348-553 3.04e-13

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: 71.16  E-value: 3.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 348 FNFLTVLGKGSFGKVLLGEQKT--TKELFAIKVLKKDViiqDDDVECTMTEKRVLALPEKPSF--LVALHSCF-QTMDR- 421
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRKNgkDGKEYAIKKFKGDK---EQYTGISQSACREIALLRELKHenVVSLVEVFlEHADKs 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 422 LYFVMEFVNggdlmYQIQQVGKF-KEPVAVFYAA--------EIAVGLFFLHSKGIIYRDLKLDNVMLERDGH----IKI 488
Cdd:cd07842  79 VYLLFDYAE-----HDLWQIIKFhRQAKRVSIPPsmvksllwQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKI 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986426 489 TDFGMCKenIF---------GDATTKTFCgtpdYIAPEIIL-YQPYGKSVDWWAYGVLLFEMLAGQPPFDGEDED 553
Cdd:cd07842 154 GDLGLAR--LFnaplkpladLDPVVVTIW----YRAPELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGREAK 222
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
468-613 3.39e-13

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: 70.47  E-value: 3.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 468 IIYRDLKLDNVMLERDGHIKITDFGMCKENIFGDATTKTfCGTPDYIAPEIIL----YQPYGKSVDWWAYGVLLFEMLAG 543
Cdd:cd06616 131 IIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSIAKTRD-AGCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATG 209
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426 544 QPPFDGedEDELFTAITE---------HNvSYPKSLSKEAVSLCKALLIKNPSKRlgctgddeSASRDIKEHPFFRRID 613
Cdd:cd06616 210 KFPYPK--WNSVFDQLTQvvkgdppilSN-SEEREFSPSFVNFVNLCLIKDESKR--------PKYKELLKHPFIKMYE 277
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
175-274 3.50e-13

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 67.35  E-value: 3.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426 175 LTIKILEAKNLIPMDPNGlSDPYVKCKLIPEdsgcksKQKTKTLRATLNPQWNETFTYKLlpGDKDRRLSIEVWDWDRTS 254
Cdd:cd04038   4 LKVRVVRGTNLAVRDFTS-SDPYVVLTLGNQ------KVKTRVIKKNLNPVWNEELTLSV--PNPMAPLKLEVFDKDTFS 74
                        90       100
                ....*....|....*....|
gi 71986426 255 RNDFMGSLSFGISELMkEAA 274
Cdd:cd04038  75 KDDSMGEAEIDLEPLV-EAA 93
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
39-90 1.09e-12

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 62.73  E-value: 1.09e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNfACPG 90
Cdd:cd20817   1 HSFQEHTFKKPTFCDVCKELLVGLSKQGLRCKNCKMNVHHKCQEGVP-DCSG 51
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
39-90 1.62e-12

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 62.31  E-value: 1.62e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPG 90
Cdd:cd20796   2 HTFVVHTYTKPTVCQHCKKLLKGLFRQGLQCKDCKFNCHKKCAEKVPKDCTG 53
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
104-153 2.08e-12

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 62.26  E-value: 2.08e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20792   2 HKFVATFFKQPTFCSHCKDFIWGLGKQGYQCQVCRFVVHKRCHEYVVFKC 51
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
39-89 7.50e-12

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. 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. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 60.36  E-value: 7.50e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACP 89
Cdd:cd20809   1 HKFIVRTFSTPTKCNHCTSLMVGLVRQGLVCEVCGYACHVSCADKAPQVCP 51
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
38-89 3.19e-11

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410356  Cd Length: 53  Bit Score: 58.86  E-value: 3.19e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71986426  38 SHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACP 89
Cdd:cd20806   1 PHNFKVHTFKGPHWCDYCGNFMWGLIAQGVKCEDCGFNAHKQCSKLVPHDCQ 52
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
35-93 4.57e-11

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410391  Cd Length: 75  Bit Score: 58.90  E-value: 4.57e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426  35 EIKSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADK 93
Cdd:cd20841   7 QIRPHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRK 65
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
36-80 8.94e-11

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 57.70  E-value: 8.94e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71986426  36 IKSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRC 80
Cdd:cd20795   1 IRPHSLFVHSYKSPTFCDFCGEMLFGLVRQGLKCEGCGLNFHKRC 45
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
35-93 2.00e-10

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 57.34  E-value: 2.00e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426  35 EIKSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADK 93
Cdd:cd20839   4 QIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRK 62
C1_PKD2_rpt1 cd20840
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
35-93 8.69e-10

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410390  Cd Length: 73  Bit Score: 55.45  E-value: 8.69e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71986426  35 EIKSHKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFACPGADK 93
Cdd:cd20840   7 QIRPHALNVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSGARK 65
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
104-153 2.27e-09

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 53.46  E-value: 2.27e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20803   2 HSFRKKTFHKPTYCHHCTDLLWGLLNQGYQCEVCNFVSHERCLKTVVTPC 51
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
46-80 1.02e-08

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410347  Cd Length: 56  Bit Score: 51.70  E-value: 1.02e-08
                        10        20        30
                ....*....|....*....|....*....|....*
gi 71986426  46 FKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRC 80
Cdd:cd20797  11 YMTPTFCDYCGEMLTGLMKQGVKCKNCRCNFHKRC 45
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
39-88 2.35e-08

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 50.49  E-value: 2.35e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd20827   2 HRFEKHNFTTPTYCDYCSSLLWGLVKTGMRCADCGYSCHEKCLEHVPKNC 51
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
175-269 7.36e-08

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 55.92  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986426  175 LTIKILEAKNLIPMDP--NGLSDPYVKCKLipEDsgcKSKQKTKTLRATLNPQWNETFtYKLLpGDKDRRLSIEVWDWDR 252
Cdd:COG5038  438 VEVKIKSAEGLKKSDStiNGTVDPYITVTF--SD---RVIGKTRVKKNTLNPVWNETF-YILL-NSFTDPLNLSLYDFNS 510
                         90
                 ....*....|....*..
gi 71986426  253 TSRNDFMGSLSFGISEL 269
Cdd:COG5038  511 FKSDKVVGSTQLDLALL 527
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
104-153 1.65e-07

first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410383  Cd Length: 58  Bit Score: 48.56  E-value: 1.65e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMC 153
Cdd:cd20833   3 HKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCSFVVHKRCHEFVTFSC 52
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
39-88 5.42e-07

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 47.05  E-value: 5.42e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71986426  39 HKFIARFFKQPTFCSHCKDFLWGITKQGFQCQVCTLVVHKRCHEFVNFAC 88
Cdd:cd20828   6 HNFEPHSFVTPTNCDYCLQILWGIVKKGMKCSECGYNCHEKCQPQVPKQC 55
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
104-154 1.93e-04

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 39.56  E-value: 1.93e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71986426 104 HKWKVQTYSSPTFCDHCGSLLYGILHQGMKCQSCDTNVHHRCVKNVPNMCG 154
Cdd:cd20794   3 HLFQAKRFNRRAVCAYCSDRIWGLGRQGYKCINCKLLVHKKCHKLVKVACG 53
 
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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