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Conserved domains on  [gi|68362740|ref|NP_008995|]
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kalirin isoform 3 [Homo sapiens]

Protein Classification

kalirin( domain architecture ID 11725713)

kalirin is a large multidomain protein containing two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it also functions as a GEF, activating Rac1, RhoA, and RhoG; typically contains spectrin-like repeats

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
993-1240 0e+00

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: 540.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAP 1152
Cdd:cd14115   81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFAAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1153 EVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTA 1232
Cdd:cd14115  161 EVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRPTA 240

                 ....*...
gi 68362740 1233 ATCLQHPW 1240
Cdd:cd14115  241 ATCLQHPW 248
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
410-544 8.36e-73

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270061  Cd Length: 140  Bit Score: 238.31  E-value: 8.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  410 LGRLQGFEGTLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGS--LTPGYMFKRSIKMNYLVLEE 487
Cdd:cd13241    1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTqfSNPGYIYKNHIKVNKMSLEE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  488 NVDNDPCKFALMNRE---TSERVVLQAANADIQQAWVQDINQVLETQRDFLNALQSPIEY 544
Cdd:cd13241   81 NVDGDPLRFALKSRDpnnPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
236-405 2.80e-50

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 175.57  E-value: 2.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    236 VLNELVQTEKDYVKDLGIVVEGFMKRIEE--KGVPEDMrgkdKIVFGNIHQIYDWHKDFFLAELEKCIQEQDRLAQLFIK 313
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    314 HERKLHIYVWYCQNKPRSEYIV-------AEYDAYFEEV-KQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAGL 385
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkknPKFRAFLEELeANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 68362740    386 ECSDIEKAVELMCLVPKRCN 405
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
SH3-RhoG_link super family cl24983
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
25-235 2.09e-43

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


The actual alignment was detected with superfamily member pfam16609:

Pssm-ID: 465196  Cd Length: 261  Bit Score: 159.20  E-value: 2.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     25 FPCRDAYSHSSSENGgKSESVANLQAQPSLNSiHSSPGPKRSTNTLKKWLTSPVRRLNSGKADGNIK----KQKKVRDGR 100
Cdd:pfam16609   17 FNHKDTLSVYSNDSI-MPGSSATLQPGHGISS-HASPGPKRPGNTLRKWLTSPVRRLSSGKADGHVKklahKHKKSREVR 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    101 KS--FDLGSPKPGDET--TPQGDSADEKSK-----------------KGWGEDEPDEESHT-PLPPPMKIFDN---DP-T 154
Cdd:pfam16609   95 KSreITAGSQKDSDDSaaTPQDETVEERVRneglssgtlskssssgmQSCGEEEGEEGADSvPLPPPMAIQQHsllQPdS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    155 QDEMSSSLLAARQASTEVPTAADLVNAIEKLVKNKLSLEGSSYRGSLkDPAGCLNEGMAPP-------TPPKNPEEEQKA 227
Cdd:pfam16609  175 QDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSV-DQGDSSSPSFNPSdnsllssSSPISEMDERRS 253

                   ....*...
gi 68362740    228 KALRGRMF 235
Cdd:pfam16609  254 SFLKKRHY 261
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
628-686 2.25e-32

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212787  Cd Length: 59  Bit Score: 119.85  E-value: 2.25e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68362740  628 SMAVIKDYYALKENEICVSQGEVVQVLAVNQQNMCLVYQPASDHSPAAEGWVPGSILAP 686
Cdd:cd11853    1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
I-set pfam07679
Immunoglobulin I-set domain;
774-868 6.05e-23

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 6.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNIldtdNSSATYTVSsCDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPL----RSSDRFKVT-YEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|....*
gi 68362740    854 TNDHGTTSTSATVKV 868
Cdd:pfam07679   76 TNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
872-963 1.63e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  872 PAAPNRPIAQERSCTSVILRWLPPSSTGNcTISGYTVEYREEGSQIWQQ-SVASTLDTYLVIEDLSPGCPYQFRVSASNP 950
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                         90
                 ....*....|...
gi 68362740  951 WGISLPSEPSEFV 963
Cdd:cd00063   80 GGESPPSESVTVT 92
 
Name Accession Description Interval E-value
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
993-1240 0e+00

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: 540.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAP 1152
Cdd:cd14115   81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFAAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1153 EVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTA 1232
Cdd:cd14115  161 EVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRPTA 240

                 ....*...
gi 68362740 1233 ATCLQHPW 1240
Cdd:cd14115  241 ATCLQHPW 248
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
987-1241 1.61e-74

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 247.83  E-value: 1.61e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkkKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:smart00220   81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDED---GHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVK 237
                           250
                    ....*....|....*..
gi 68362740    1225 DFRRRPTAATCLQHPWL 1241
Cdd:smart00220  238 DPEKRLTAEEALQHPFF 254
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
410-544 8.36e-73

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 238.31  E-value: 8.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  410 LGRLQGFEGTLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGS--LTPGYMFKRSIKMNYLVLEE 487
Cdd:cd13241    1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTqfSNPGYIYKNHIKVNKMSLEE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  488 NVDNDPCKFALMNRE---TSERVVLQAANADIQQAWVQDINQVLETQRDFLNALQSPIEY 544
Cdd:cd13241   81 NVDGDPLRFALKSRDpnnPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
236-405 2.80e-50

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 175.57  E-value: 2.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    236 VLNELVQTEKDYVKDLGIVVEGFMKRIEE--KGVPEDMrgkdKIVFGNIHQIYDWHKDFFLAELEKCIQEQDRLAQLFIK 313
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    314 HERKLHIYVWYCQNKPRSEYIV-------AEYDAYFEEV-KQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAGL 385
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkknPKFRAFLEELeANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 68362740    386 ECSDIEKAVELMCLVPKRCN 405
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
233-405 3.25e-47

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 167.09  E-value: 3.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  233 RMFVLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPeDMRGKDKIVFGNIHQIYDWHKDFfLAELEKCIQEQD----RLA 308
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP-LSPEEVELLFGNIEEIYEFHRIF-LKSLEERVEEWDksgpRIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  309 QLFIKHERKLHIYVWYCQNKPRSEYIVAEYDA---YFEEVKQEIN---QRLTLSDFLIKPIQRITKYQLLLKDFLRYSEK 382
Cdd:cd00160   79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnkFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                        170       180
                 ....*....|....*....|...
gi 68362740  383 AGLECSDIEKAVELMCLVPKRCN 405
Cdd:cd00160  159 GHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
236-406 4.81e-47

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 166.32  E-value: 4.81e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     236 VLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPEDMRGKDKIvFGNIHQIYDWHKDFfLAELEKCIQE----QDRLAQLF 311
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL-FGNIEEIYEFHRDF-LDELEERIEEwddsVERIGDVF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     312 IKHERKLHIYVWYCQNKPRSEYIVAE------YDAYFEEV-KQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAG 384
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALELLKKlkknprFQKFLKEIeSSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                           170       180
                    ....*....|....*....|..
gi 68362740     385 LECSDIEKAVELMCLVPKRCND 406
Cdd:smart00325  159 EDREDLKKALKAIKELANQVNE 180
Pkinase pfam00069
Protein kinase domain;
987-1241 2.14e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 160.49  E-value: 2.14e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIkkeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALqylhncrvahldiKPENLLidlripvprvklidledavqisghfhiHHL 1143
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------ESGSSL---------------------------TTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFcGVSNAARDFINVILQ 1223
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPS-NLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 68362740   1224 EDFRRRPTAATCLQHPWL 1241
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
25-235 2.09e-43

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 159.20  E-value: 2.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     25 FPCRDAYSHSSSENGgKSESVANLQAQPSLNSiHSSPGPKRSTNTLKKWLTSPVRRLNSGKADGNIK----KQKKVRDGR 100
Cdd:pfam16609   17 FNHKDTLSVYSNDSI-MPGSSATLQPGHGISS-HASPGPKRPGNTLRKWLTSPVRRLSSGKADGHVKklahKHKKSREVR 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    101 KS--FDLGSPKPGDET--TPQGDSADEKSK-----------------KGWGEDEPDEESHT-PLPPPMKIFDN---DP-T 154
Cdd:pfam16609   95 KSreITAGSQKDSDDSaaTPQDETVEERVRneglssgtlskssssgmQSCGEEEGEEGADSvPLPPPMAIQQHsllQPdS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    155 QDEMSSSLLAARQASTEVPTAADLVNAIEKLVKNKLSLEGSSYRGSLkDPAGCLNEGMAPP-------TPPKNPEEEQKA 227
Cdd:pfam16609  175 QDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSV-DQGDSSSPSFNPSdnsllssSSPISEMDERRS 253

                   ....*...
gi 68362740    228 KALRGRMF 235
Cdd:pfam16609  254 SFLKKRHY 261
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
987-1234 3.72e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 3.72e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEArerfRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIHH 1142
Cdd:COG0515   89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT---PDGRVKLIDFGIARALGGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 --LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINV 1220
Cdd:COG0515  166 gtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245
                        250
                 ....*....|....
gi 68362740 1221 ILQEDFRRRPTAAT 1234
Cdd:COG0515  246 ALAKDPEERYQSAA 259
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
628-686 2.25e-32

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 119.85  E-value: 2.25e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68362740  628 SMAVIKDYYALKENEICVSQGEVVQVLAVNQQNMCLVYQPASDHSPAAEGWVPGSILAP 686
Cdd:cd11853    1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
991-1229 1.49e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 118.00  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   991 NEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGhfHIHHLLGN 1146
Cdd:PTZ00263  104 ELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVPD--RTFTLCGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQEDF 1226
Cdd:PTZ00263  179 PEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN----WFDGRARDLVKGLLQTDH 254

                  ...
gi 68362740  1227 RRR 1229
Cdd:PTZ00263  255 TKR 257
I-set pfam07679
Immunoglobulin I-set domain;
774-868 6.05e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 6.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNIldtdNSSATYTVSsCDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPL----RSSDRFKVT-YEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|....*
gi 68362740    854 TNDHGTTSTSATVKV 868
Cdd:pfam07679   76 TNSAGEAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
872-963 1.63e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  872 PAAPNRPIAQERSCTSVILRWLPPSSTGNcTISGYTVEYREEGSQIWQQ-SVASTLDTYLVIEDLSPGCPYQFRVSASNP 950
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                         90
                 ....*....|...
gi 68362740  951 WGISLPSEPSEFV 963
Cdd:cd00063   80 GGESPPSESVTVT 92
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
766-868 1.14e-16

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 76.28  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  766 PNFIQEvapeflvPLVDVTCLLGDTVILQCKVCGRPKPTITWKgpdQNILDTDNSSATYTVsscdsGEITLKICNLMPQD 845
Cdd:cd20978    1 PKFIQK-------PEKNVVVKGGQDVTLPCQVTGVPQPKITWL---HNGKPLQGPMERATV-----EDGTLTIINVQPED 65
                         90       100
                 ....*....|....*....|...
gi 68362740  846 SGIYTCIATNDHGTTSTSATVKV 868
Cdd:cd20978   66 TGYYGCVATNEIGDIYTETLLHV 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
782-868 2.64e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.46  E-value: 2.64e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     782 DVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNssaTYTVSScDSGEITLKICNLMPQDSGIYTCIATNDHGTTS 861
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG---RFSVSR-SGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                    ....*..
gi 68362740     862 TSATVKV 868
Cdd:smart00410   79 SGTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
872-954 3.58e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 3.58e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     872 PAAPNRPIAQERSCTSVILRWLPPSSTGNCT-ISGYTVEYREEGSQiWQQSVASTLDTYLVIEDLSPGCPYQFRVSASNP 950
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 68362740     951 WGIS 954
Cdd:smart00060   80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
787-963 3.69e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.80  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  787 LGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCI--ATNDHGTTSTSA 864
Cdd:COG3401  143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRvaATDTGGESAPSN 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  865 TVKVQGVPAAPNRPI---AQERSCTSVILRWLPPSSTGnctISGYTVEYREEGSQIWQQsVASTLDTYLVIEDLSPGCPY 941
Cdd:COG3401  223 EVSVTTPTTPPSAPTgltATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTK-VATVTTTSYTDTGLTNGTTY 298
                        170       180
                 ....*....|....*....|..
gi 68362740  942 QFRVSASNPWGIslPSEPSEFV 963
Cdd:COG3401  299 YYRVTAVDAAGN--ESAPSNVV 318
fn3 pfam00041
Fibronectin type III domain;
874-957 4.02e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 4.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    874 APNRPIAQERSCTSVILRWLPPSsTGNCTISGYTVEYREEGSQ-IWQ-QSVASTLDTYlVIEDLSPGCPYQFRVSASNPW 951
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNeITVPGTTTSV-TLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 68362740    952 GISLPS 957
Cdd:pfam00041   80 GEGPPS 85
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
224-397 5.47e-11

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 67.61  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  224 EQKAKALRGRMFVLNELVQTEKDYVKDLGIVVEGFMKRIEE-KGVPEDMRGK-DKIVFGNIHQIYDWHKDFF--LAELEK 299
Cdd:COG5422  476 ESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEEsNIIPENARRNfIKHVFANINEIYAVNSKLLkaLTNRQC 555
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  300 CIQEQDRLAQLFIKHERKLHIYVWYCQNKPRSEYI----------VAEYDAYFEEVKQeiNQRLTLSDFLIKPIQRITKY 369
Cdd:COG5422  556 LSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEfereksvnpnFARFDHEVERLDE--SRKLELDGYLTKPTTRLARY 633
                        170       180
                 ....*....|....*....|....*...
gi 68362740  370 QLLLKDFLRYSEKAGLECSDIEKAVELM 397
Cdd:COG5422  634 PLLLEEVLKFTDPDNPDTEDIPKVIDML 661
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
993-1187 1.48e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 59.04  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   993 IGRGRFSIVkkciHKA--TR--KDVAVKFVSKKMKKKEQA-------AHEAAllqHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:NF033483   15 IGRGGMAEV----YLAkdTRldRDVAVKVLRPDLARDPEFvarfrreAQSAA---SLSHPNIVSVYDVGEDGGIPYIVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1062 LMDdGRLL-DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGH--F 1138
Cdd:NF033483   88 YVD-GRTLkDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIARALSSTtmT 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 68362740  1139 HIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDES 1187
Cdd:NF033483  164 QTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
433-528 1.12e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 45.62  E-value: 1.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     433 YVIELDAGMQSRTKERRVFLFEQIVIFSellRKGSLTPGYMFKRSIKMNYLVLEENVDND----PCKFALMNRETsERVV 508
Cdd:smart00233    6 WLYKKSGGGKKSWKKRYFVLFNSTLLYY---KSKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIKTSDR-KTLL 81
                            90       100
                    ....*....|....*....|
gi 68362740     509 LQAANADIQQAWVQDINQVL 528
Cdd:smart00233   82 LQAESEEEREKWVEALRKAI 101
 
Name Accession Description Interval E-value
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
993-1240 0e+00

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: 540.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAP 1152
Cdd:cd14115   81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVHHLLGNPEFAAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1153 EVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTA 1232
Cdd:cd14115  161 EVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQEDPRRRPTA 240

                 ....*...
gi 68362740 1233 ATCLQHPW 1240
Cdd:cd14115  241 ATCLQHPW 248
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
979-1241 6.19e-132

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: 405.13  E-value: 6.19e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  979 WKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYIL 1058
Cdd:cd14113    1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1059 ILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHF 1138
Cdd:cd14113   81 VLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFI 1218
Cdd:cd14113  161 YIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFV 240
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14113  241 CFLLQMDPAKRPSAALCLQEQWL 263
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
993-1240 3.58e-126

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: 388.93  E-value: 3.58e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAP 1152
Cdd:cd14006   81 AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADR-PSPQIKIIDFGLARKLNPGEELKEIFGTPEFVAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1153 EVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV--CRVDFSFPheYFCGVSNAARDFINVILQEDFRRRP 1230
Cdd:cd14006  160 EIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANIsaCRVDFSEE--YFSSVSQEAKDFIRKLLVKEPRKRP 237
                        250
                 ....*....|
gi 68362740 1231 TAATCLQHPW 1240
Cdd:cd14006  238 TAQEALQHPW 247
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
981-1241 1.64e-78

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: 259.73  E-value: 1.64e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV-------SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP 1053
Cdd:cd14105    1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIkkrrskaSRRGVSREDIEREVSILRQVLHPNIITLHDVFENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAV 1132
Cdd:cd14105   81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNVPIPRIKLIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd14105  161 KIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14105  241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
981-1241 2.57e-76

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: 253.79  E-value: 2.57e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV-------SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP 1053
Cdd:cd14194    1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIkkrrtksSRRGVSREDIEREVSILKEIQHPNVITLHEVYENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAV 1132
Cdd:cd14194   81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVPKPRIKIIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd14194  161 KIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSA 240
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14194  241 LAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
987-1241 1.61e-74

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 247.83  E-value: 1.61e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkkKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:smart00220   81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDED---GHVKLADFGLARQLDPGEKLTTFV 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:smart00220  158 GTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLVK 237
                           250
                    ....*....|....*..
gi 68362740    1225 DFRRRPTAATCLQHPWL 1241
Cdd:smart00220  238 DPEKRLTAEEALQHPFF 254
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
980-1241 1.19e-73

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: 246.11  E-value: 1.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  980 KENFDSAYT-ELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALL-QHLQHPQYITLHDTYESPT 1054
Cdd:cd14106    2 TENINEVYTvESTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNeilHEIAVLeLCKDCPRVVNLHEVYETRS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 SYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQI 1134
Cdd:cd14106   82 ELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1135 SGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAA 1214
Cdd:cd14106  162 GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLA 241
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14106  242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
981-1241 2.98e-73

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: 244.87  E-value: 2.98e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV-------SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP 1053
Cdd:cd14196    1 QKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIkkrqsraSRRGVSREEIEREVSILRQVLHPNIITLHDVYENR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAV 1132
Cdd:cd14196   81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIPHIKLIDFGLAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd14196  161 EIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14196  241 LAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
987-1240 3.04e-73

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: 244.31  E-value: 3.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMlrrEIEILKRLDHPNIVKLYEVFEDDKNLYLVMELC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHL 1143
Cdd:cd05117   82 TGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGEKLKTV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQ 1223
Cdd:cd05117  162 CGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLLV 241
                        250
                 ....*....|....*..
gi 68362740 1224 EDFRRRPTAATCLQHPW 1240
Cdd:cd05117  242 VDPKKRLTAAEALNHPW 258
PH2_Kalirin_Trio_p63RhoGEF cd13241
p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor ...
410-544 8.36e-73

p63RhoGEF pleckstrin homology (PH) domain, repeat 2; The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric G protein, Galphaq and linking Galphaq-coupled receptors (GPCRs) to the activation of RhoA. The Dbl(DH) and PH domains of p63RhoGEF interact with the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270061  Cd Length: 140  Bit Score: 238.31  E-value: 8.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  410 LGRLQGFEGTLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGS--LTPGYMFKRSIKMNYLVLEE 487
Cdd:cd13241    1 VGRLQGFDGKITAQGKLLLQGTLLVSEPSAGLLQKGKERRVFLFEQIIIFSEILGKKTqfSNPGYIYKNHIKVNKMSLEE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  488 NVDNDPCKFALMNRE---TSERVVLQAANADIQQAWVQDINQVLETQRDFLNALQSPIEY 544
Cdd:cd13241   81 NVDGDPLRFALKSRDpnnPSETFILQAASPEVRQEWVDTINQILDTQRDFLKALQSPIAY 140
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
981-1242 3.97e-72

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: 241.83  E-value: 3.97e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV-------SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP 1053
Cdd:cd14195    1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIkkrrlssSRRGVSREEIEREVNILREIQHPNIITLHDIFENK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAV 1132
Cdd:cd14195   81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVPNPRIKLIDFGIAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd14195  161 KIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSE 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14195  241 LAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
993-1241 5.63e-72

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: 240.59  E-value: 5.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIkCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFA 1150
Cdd:cd14103   81 VVDDDfELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILC-VSRTGNQIKIIDFGLARKYDPDKKLKVLFGTPEFV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1151 APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRP 1230
Cdd:cd14103  160 APEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKDPRKRM 239
                        250
                 ....*....|.
gi 68362740 1231 TAATCLQHPWL 1241
Cdd:cd14103  240 SAAQCLQHPWL 250
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
992-1241 4.30e-61

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: 210.56  E-value: 4.30e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQ-HPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd14197   16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmEIIHEIAVLELAQaNPWVINLHEVYETASEMILVLEYAAGGE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDY-LMNHDELMEEK-VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLG 1145
Cdd:cd14197   96 IFNQcVADREEAFKEKdVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREIMG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQED 1225
Cdd:cd14197  176 TPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKTLLIKK 255
                        250
                 ....*....|....*.
gi 68362740 1226 FRRRPTAATCLQHPWL 1241
Cdd:cd14197  256 PENRATAEDCLKHPWL 271
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
981-1241 6.81e-59

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: 204.00  E-value: 6.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYT-ELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQ-HPQYITLHDTYESPTS 1055
Cdd:cd14198    3 DNFNNFYIlTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAeilHEIAVLELAKsNPRVVNLHEVYETTSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILILELMDDGRLLDYLMN--HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQ 1133
Cdd:cd14198   83 IILILEYAAGGEIFNLCVPdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNA 1213
Cdd:cd14198  163 IGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQL 242
                        250       260
                 ....*....|....*....|....*...
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14198  243 ATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
987-1241 2.42e-58

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: 202.04  E-value: 2.42e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd14114    4 YDILEELGTGAFGVVHRCTERATGNNFAAKFImTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELM-EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:cd14114   84 GELFERIAAEHYKMsEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTK-RSNEVKLIDFGLATHLDPKESVKVTT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:cd14114  163 GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEAKDFIRKLLLA 242
                        250
                 ....*....|....*..
gi 68362740 1225 DFRRRPTAATCLQHPWL 1241
Cdd:cd14114  243 DPNKRMTIHQALEHPWL 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
993-1240 9.28e-57

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: 196.97  E-value: 9.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14003    8 LGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKikrEIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGELF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LedavqiSGHFHIHHLL--- 1144
Cdd:cd14003   88 DYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKN---GNLKIIDfgL------SNEFRGGSLLktf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 -GNPEFAAPEVIQGIPVsLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVI 1221
Cdd:cd14003  159 cGTPAYAAPEVLLGRKY-DGpkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSH----LSPDARDLIRRM 233
                        250
                 ....*....|....*....
gi 68362740 1222 LQEDFRRRPTAATCLQHPW 1240
Cdd:cd14003  234 LVVDPSKRITIEEILNHPW 252
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
985-1241 4.67e-56

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: 195.49  E-value: 4.67e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd14107    2 SVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:cd14107   82 SEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILM-VSPTREDIKICDFGFAQEITPSEHQFSKY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:cd14107  161 GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDAKDFIKRVLQP 240
                        250
                 ....*....|....*..
gi 68362740 1225 DFRRRPTAATCLQHPWL 1241
Cdd:cd14107  241 DPEKRPSASECLSHEWF 257
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
992-1242 2.47e-54

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: 191.23  E-value: 2.47e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14104    7 ELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFER 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPvPRVKLIDLEDAVQISGHFHIHHLLGNPEFA 1150
Cdd:cd14104   87 ITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRG-SYIKIIEFGQSRQLKPGDKFRLQYTSAEFY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1151 APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRP 1230
Cdd:cd14104  166 APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRM 245
                        250
                 ....*....|..
gi 68362740 1231 TAATCLQHPWLQ 1242
Cdd:cd14104  246 TAQEALNHPWLK 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
993-1242 7.81e-54

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: 188.84  E-value: 7.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS----KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14007    8 LGKGKFGNVYLAREKKSGFIVALKVISksqlQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHfHIHHLLGNPE 1148
Cdd:cd14007   88 YKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSN---GELKLADFGWSVHAPSN-RRKTFCGTLD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 FAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPhEYfcgVSNAARDFINVILQEDFRR 1228
Cdd:cd14007  164 YLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFP-SS---VSPEAKDLISKLLQKDPSK 239
                        250
                 ....*....|....
gi 68362740 1229 RPTAATCLQHPWLQ 1242
Cdd:cd14007  240 RLSLEQVLNHPWIK 253
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
987-1241 2.85e-53

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: 187.52  E-value: 2.85e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd14191    4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFkAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:cd14191   84 GELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMC-VNKTGTKIKLIDFGLARRLENAGSLKVLF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:cd14191  163 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKK 242
                        250
                 ....*....|....*..
gi 68362740 1225 DFRRRPTAATCLQHPWL 1241
Cdd:cd14191  243 DMKARLTCTQCLQHPWL 259
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
992-1241 4.10e-53

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: 186.65  E-value: 4.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDy 1071
Cdd:cd14108    9 EIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEELLER- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAA 1151
Cdd:cd14108   88 ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLM-ADQKTDQVRICDFGNAQELTPNEPQYCKYGTPEFVA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1152 PEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDfRRRPT 1231
Cdd:cd14108  167 PEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFIIKVLVSD-RLRPD 245
                        250
                 ....*....|
gi 68362740 1232 AATCLQHPWL 1241
Cdd:cd14108  246 AEETLEHPWF 255
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
987-1255 4.54e-51

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: 182.06  E-value: 4.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHeaALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIE--ILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPvPRVKLIDLEDAVQISghfHIHHLL 1144
Cdd:cd14091   80 ELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYadESGDP-ESLRICDFGFAKQLR---AENGLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNP----EFAAPEVI--QGIPVSlgTDIWSIGVLTYVMLSGVSPFL---DESKEE--TCINVCRVDFSFPHeyFCGVSNA 1213
Cdd:cd14091  156 MTPcytaNFVAPEVLkkQGYDAA--CDIWSLGVLLYTMLAGYTPFAsgpNDTPEVilARIGSGKIDLSGGN--WDHVSDS 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHPWL-QPHNGSYSKIPLDT 1255
Cdd:cd14091  232 AKDLVRKMLHVDPSQRPTAAQVLQHPWIrNRDSLPQRQLTDPQ 274
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
993-1241 2.12e-50

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: 179.35  E-value: 2.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTGLKLAAKVInKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFER 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPvPRVKLIDLEDAVQISGHFHIHHLLGNPEFA 1150
Cdd:cd14190   92 IVDEDyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTG-HQVKIIDFGLARRYNPREKLKVNFGTPEFL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1151 APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRP 1230
Cdd:cd14190  171 SPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSARM 250
                        250
                 ....*....|.
gi 68362740 1231 TAATCLQHPWL 1241
Cdd:cd14190  251 SATQCLKHPWL 261
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
236-405 2.80e-50

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 175.57  E-value: 2.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    236 VLNELVQTEKDYVKDLGIVVEGFMKRIEE--KGVPEDMrgkdKIVFGNIHQIYDWHKDFFLAELEKCIQEQDRLAQLFIK 313
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKplSESEEEI----KTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDIFLK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    314 HERKLHIYVWYCQNKPRSEYIV-------AEYDAYFEEV-KQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAGL 385
Cdd:pfam00621   77 FAPGFKVYSTYCSNYPKALKLLkkllkknPKFRAFLEELeANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHP 156
                          170       180
                   ....*....|....*....|
gi 68362740    386 ECSDIEKAVELMCLVPKRCN 405
Cdd:pfam00621  157 DYEDLKKALEAIKEVAKQIN 176
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
993-1240 3.89e-49

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: 175.59  E-value: 3.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd14095    8 IGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGGDLFD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLRIpvpRVKLIDLEDAVQISGhfHIHHLLGN 1146
Cdd:cd14095   88 AITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSK---SLKLADFGLATEVKE--PLFTVCGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL--DESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:cd14095  163 PTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLISRMLVV 242
                        250
                 ....*....|....*.
gi 68362740 1225 DFRRRPTAATCLQHPW 1240
Cdd:cd14095  243 DPEKRYSAGQVLDHPW 258
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
993-1241 8.99e-49

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: 174.72  E-value: 8.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKIIkARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFDR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFA 1150
Cdd:cd14193   92 IIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSR-EANQVKIIDFGLARRYKPREKLRVNFGTPEFL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1151 APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRP 1230
Cdd:cd14193  171 APEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWRM 250
                        250
                 ....*....|.
gi 68362740 1231 TAATCLQHPWL 1241
Cdd:cd14193  251 SASEALKHPWL 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
985-1241 1.10e-47

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: 171.30  E-value: 1.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNE---IGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILIL 1060
Cdd:cd14192    1 NSYYAVCPhevLGGGRFGQVHKCTELSTGLTLAAKIIKvKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGRLLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHFH 1139
Cdd:cd14192   81 EYVDGGELFDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILC-VNSTGNQIKIIDFGLARRYKPREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFIN 1219
Cdd:cd14192  160 LKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFIS 239
                        250       260
                 ....*....|....*....|..
gi 68362740 1220 VILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14192  240 RLLVKEKSCRMSATQCLKHEWL 261
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
233-405 3.25e-47

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 167.09  E-value: 3.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  233 RMFVLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPeDMRGKDKIVFGNIHQIYDWHKDFfLAELEKCIQEQD----RLA 308
Cdd:cd00160    1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLP-LSPEEVELLFGNIEEIYEFHRIF-LKSLEERVEEWDksgpRIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  309 QLFIKHERKLHIYVWYCQNKPRSEYIVAEYDA---YFEEVKQEIN---QRLTLSDFLIKPIQRITKYQLLLKDFLRYSEK 382
Cdd:cd00160   79 DVFLKLAPFFKIYSEYCSNHPDALELLKKLKKfnkFFQEFLEKAEsecGRLKLESLLLKPVQRLTKYPLLLKELLKHTPD 158
                        170       180
                 ....*....|....*....|...
gi 68362740  383 AGLECSDIEKAVELMCLVPKRCN 405
Cdd:cd00160  159 GHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
236-406 4.81e-47

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 166.32  E-value: 4.81e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     236 VLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPEDMRGKDKIvFGNIHQIYDWHKDFfLAELEKCIQE----QDRLAQLF 311
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKLLSPNELETL-FGNIEEIYEFHRDF-LDELEERIEEwddsVERIGDVF 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     312 IKHERKLHIYVWYCQNKPRSEYIVAE------YDAYFEEV-KQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAG 384
Cdd:smart00325   79 LKLEEFFKIYSEYCSNHPDALELLKKlkknprFQKFLKEIeSSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDH 158
                           170       180
                    ....*....|....*....|..
gi 68362740     385 LECSDIEKAVELMCLVPKRCND 406
Cdd:smart00325  159 EDREDLKKALKAIKELANQVNE 180
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
983-1241 6.15e-47

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: 169.46  E-value: 6.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYtELNEI-GRGRFSIVKKCIHKATRKDVAVKF--VSKKMKKKEQAAH-------EAALLQHLQ-HPQYITLHDTYE 1051
Cdd:cd14093    1 FYAKY-EPKEIlGRGVSSTVRRCIEKETGQEFAVKIidITGEKSSENEAEElreatrrEIEILRQVSgHPNIIELHDVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1052 SPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDA 1131
Cdd:cd14093   80 SPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL---NVKISDFGFA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 VQISGHFHIHHLLGNPEFAAPEVIQ-----GIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHE 1205
Cdd:cd14093  157 TRLDEGEKLRELCGTPGYLAPEVLKcsmydNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSP 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 68362740 1206 YFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14093  237 EWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
987-1240 1.28e-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: 168.42  E-value: 1.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-----KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkrkvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHFHIH 1141
Cdd:cd14098   82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPV-IVKISDFGLAKVIHTGTFLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNPEFAAPEVIQGIPVSLG------TDIWSIGVLTYVMLSGVSPFlDESKEETCIN-VCRVDFSFPHEYFCGVSNAA 1214
Cdd:cd14098  161 TFCGTMAYLAPEILMSKEQNLQggysnlVDMWSVGCLVYVMLTGALPF-DGSSQLPVEKrIRKGRYTQPPLVDFNISEEA 239
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd14098  240 IDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
993-1240 4.91e-46

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: 166.39  E-value: 4.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd14083   11 LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSleNEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGELFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----DLRIPVPRVKLIDLEDAVQISGhfhihhLLG 1145
Cdd:cd14083   91 RIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspdeDSKIMISDFGLSKMEDSGVMST------ACG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQED 1225
Cdd:cd14083  165 TPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDSAKDFIRHLMEKD 244
                        250
                 ....*....|....*
gi 68362740 1226 FRRRPTAATCLQHPW 1240
Cdd:cd14083  245 PNKRYTCEQALEHPW 259
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
993-1241 5.81e-46

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: 166.27  E-value: 5.81e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLmkveREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDA-VQISGhfhihHLL--- 1144
Cdd:cd14081   89 FDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKN---NIKIADFGMAsLQPEG-----SLLets 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 -GNPEFAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVIL 1222
Cdd:cd14081  161 cGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHF----ISPDAQDLLRRML 236
                        250
                 ....*....|....*....
gi 68362740 1223 QEDFRRRPTAATCLQHPWL 1241
Cdd:cd14081  237 EVNPEKRITIEEIKKHPWF 255
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
984-1241 6.02e-46

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: 166.99  E-value: 6.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd14169    2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMveNEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----DLRIPVPRVKLIDLEDAVQISG 1136
Cdd:cd14169   82 LVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYatpfeDSKIMISDFGLSKIEAQGMLST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 hfhihhLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARD 1216
Cdd:cd14169  162 ------ACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKD 235
                        250       260
                 ....*....|....*....|....*
gi 68362740 1217 FINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14169  236 FIRHLLERDPEKRFTCEQALQHPWI 260
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
992-1241 1.11e-45

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: 166.83  E-value: 1.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14086    8 ELGKGAFSVVRRCVQKSTGQEFAAKIIntkKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISG-HFHIHHLLGNP 1147
Cdd:cd14086   88 FEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGdQQAWFGFAGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFR 1227
Cdd:cd14086  168 GYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKDLINQMLTVNPA 247
                        250
                 ....*....|....
gi 68362740 1228 RRPTAATCLQHPWL 1241
Cdd:cd14086  248 KRITAAEALKHPWI 261
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
993-1255 8.70e-45

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: 164.78  E-value: 8.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMkkkeQAAHEAALLQHLQ-HPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14092   14 LGDGSFSVCRKCVHKKTGQEFAVKIVSRRL----DTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGGELLER 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDledavqisghFHIHHLLGNPE--- 1148
Cdd:cd14092   90 IRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVD----------FGFARLKPENQplk 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 -------FAAPEVIQGIPVSLG----TDIWSIGVLTYVMLSGVSPF----LDESKEETCINVCRVDFSFPHEYFCGVSNA 1213
Cdd:cd14092  160 tpcftlpYAAPEVLKQALSTQGydesCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDGEEWKNVSSE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHPWLQPHNgSYSKIPLDT 1255
Cdd:cd14092  240 AKSLIQGLLTVDPSKRLTMSELRNHPWLQGSS-SPSSTPLMT 280
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
987-1241 9.48e-45

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: 162.68  E-value: 9.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHF--HIHHLL 1144
Cdd:cd14111   85 ELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT---NLNAIKIVDFGSAQSFNPLSlrQLGRRT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEET--CINVCRVDfsfPHEYFCGVSNAARDFINVIL 1222
Cdd:cd14111  162 GTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETeaKILVAKFD---AFKLYPNVSQSASLFLKKVL 238
                        250
                 ....*....|....*....
gi 68362740 1223 QEDFRRRPTAATCLQHPWL 1241
Cdd:cd14111  239 SSYPWSRPTTKDCFAHAWL 257
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
987-1241 1.53e-44

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: 161.99  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH-EAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILnEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELM-EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:cd05122   82 GSLKDLLKNTNKTLtEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD---GEVKLIDFGLSAQLSDGKTRNTFV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF-SFPHEYFcgVSNAARDFINVILQ 1223
Cdd:cd05122  159 GTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPpGLRNPKK--WSKEFKDFLKKCLQ 236
                        250
                 ....*....|....*...
gi 68362740 1224 EDFRRRPTAATCLQHPWL 1241
Cdd:cd05122  237 KDPEKRPTAEQLLKHPFI 254
Pkinase pfam00069
Protein kinase domain;
987-1241 2.14e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 160.49  E-value: 2.14e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIkkeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALqylhncrvahldiKPENLLidlripvprvklidledavqisghfhiHHL 1143
Cdd:pfam00069   81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------ESGSSL---------------------------TTF 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFcGVSNAARDFINVILQ 1223
Cdd:pfam00069  121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPS-NLSEEAKDLLKKLLK 199
                          250
                   ....*....|....*...
gi 68362740   1224 EDFRRRPTAATCLQHPWL 1241
Cdd:pfam00069  200 KDPSKRLTATQALQHPWF 217
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
980-1241 3.44e-44

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: 161.35  E-value: 3.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  980 KENFDsaYTELneIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYI 1057
Cdd:cd14167    2 RDIYD--FREV--LGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSieNEIAVLHKIKHPNIVALDDIYESGGHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----DLRIPVPRVKLIDLEDAV 1132
Cdd:cd14167   78 LIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYysldeDSKIMISDFGLSKIEGSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QIsghfhIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd14167  158 SV-----MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISD 232
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14167  233 SAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
993-1239 4.20e-44

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: 159.36  E-value: 4.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIpkEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGH---FHIHHLLGN 1146
Cdd:cd00180   81 LLKENKGPLSEEEAlSILRQLLSALEYLHSNGIIHRDLKPENILLDSD---GTVKLADFGLAKDLDSDdslLKTTGGTTP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMlsgvspfldeskeetcinvcrvdfsfpheyfcgvsNAARDFINVILQEDF 1226
Cdd:cd00180  158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRMLQYDP 202
                        250
                 ....*....|...
gi 68362740 1227 RRRPTAATCLQHP 1239
Cdd:cd00180  203 KKRPSAKELLEHL 215
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
983-1266 9.51e-44

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: 161.15  E-value: 9.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKkEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14085    1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDK-KIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHH 1142
Cdd:cd14085   80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQVTMKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCIN-VCRVDFSFPHEYFCGVSNAARDFINVI 1221
Cdd:cd14085  160 VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKrILNCDYDFVSPWWDDVSLNAKDLVKKL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 68362740 1222 LQEDFRRRPTAATCLQHPWLQPHNGSYSKIPLDTSRLACFIERRK 1266
Cdd:cd14085  240 IVLDPKKRLTTQQALQHPWVTGKAANFAHMDTAQKKLQEFNARRK 284
SH3-RhoG_link pfam16609
SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved ...
25-235 2.09e-43

SH3-RhoGEF linking unstructured region; This family of natively unstructured but conserved residues from higher eukaryotes is found to lie between an SH3 pfam00018 and the RhoGEF, pfam00621, domains. It is serine-rich and likely to be acidic and natively unstructured.


Pssm-ID: 465196  Cd Length: 261  Bit Score: 159.20  E-value: 2.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     25 FPCRDAYSHSSSENGgKSESVANLQAQPSLNSiHSSPGPKRSTNTLKKWLTSPVRRLNSGKADGNIK----KQKKVRDGR 100
Cdd:pfam16609   17 FNHKDTLSVYSNDSI-MPGSSATLQPGHGISS-HASPGPKRPGNTLRKWLTSPVRRLSSGKADGHVKklahKHKKSREVR 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    101 KS--FDLGSPKPGDET--TPQGDSADEKSK-----------------KGWGEDEPDEESHT-PLPPPMKIFDN---DP-T 154
Cdd:pfam16609   95 KSreITAGSQKDSDDSaaTPQDETVEERVRneglssgtlskssssgmQSCGEEEGEEGADSvPLPPPMAIQQHsllQPdS 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    155 QDEMSSSLLAARQASTEVPTAADLVNAIEKLVKNKLSLEGSSYRGSLkDPAGCLNEGMAPP-------TPPKNPEEEQKA 227
Cdd:pfam16609  175 QDDKTSSRLFVRPSSSETPSAAELVSAIEELVKSKMALEDRPSSLSV-DQGDSSSPSFNPSdnsllssSSPISEMDERRS 253

                   ....*...
gi 68362740    228 KALRGRMF 235
Cdd:pfam16609  254 SFLKKRHY 261
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
987-1233 3.65e-43

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: 158.13  E-value: 3.65e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFrerfLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLID--LEDAVQISGHFHI 1140
Cdd:cd14014   82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLT---EDGRVKLTDfgIARALGDSGLTQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINV 1220
Cdd:cd14014  159 GSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDAIILR 238
                        250
                 ....*....|...
gi 68362740 1221 ILQEDFRRRPTAA 1233
Cdd:cd14014  239 ALAKDPEERPQSA 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
987-1234 3.72e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 3.72e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEArerfRREARALARLNHPNIVRVYDVGEEDGRPYLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIHH 1142
Cdd:COG0515   89 VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT---PDGRVKLIDFGIARALGGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 --LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINV 1220
Cdd:COG0515  166 gtVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLR 245
                        250
                 ....*....|....
gi 68362740 1221 ILQEDFRRRPTAAT 1234
Cdd:COG0515  246 ALAKDPEERYQSAA 259
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
993-1241 1.23e-42

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: 156.92  E-value: 1.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd14087    9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELFDRI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFH--IHHLLGNPEFA 1150
Cdd:cd14087   89 IAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKKGPNclMKTTCGTPEYI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1151 APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRP 1230
Cdd:cd14087  169 APEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLLTVNPGERL 248
                        250
                 ....*....|.
gi 68362740 1231 TAATCLQHPWL 1241
Cdd:cd14087  249 SATQALKHPWI 259
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
991-1241 4.84e-42

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: 154.98  E-value: 4.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVkkciHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYE-SPTSYILILELMDDGRLL 1069
Cdd:cd14109   10 EDEKRAAQGAP----FHVTERSTGRNFLAQLRYGDPFLMREVDIHNSLDHPNIVQMHDAYDdEKLAVTVIDNLASTIELV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 --DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlripVPRVKLIDLEDAVQISGHFHIHHLLGNP 1147
Cdd:cd14109   86 rdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ----DDKLKLADFGQSRRLLRGKLTTLIYGSP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFR 1227
Cdd:cd14109  162 EFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLVYIPE 241
                        250
                 ....*....|....
gi 68362740 1228 RRPTAATCLQHPWL 1241
Cdd:cd14109  242 SRLTVDEALNHPWF 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
981-1241 5.30e-42

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: 155.63  E-value: 5.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---------EAALLQHLQHPQYITLHDTYE 1051
Cdd:cd14084    2 KELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREinkprnietEIEILKKLSHPCIIKIEDFFD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1052 SPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDA 1131
Cdd:cd14084   82 AEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFGLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 vQISGHFHIHHLL-GNPEFAAPEVIQ---GIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCIN-VCRVDFSFPHEY 1206
Cdd:cd14084  162 -KILGETSLMKTLcGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEqILSGKYTFIPKA 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 68362740 1207 FCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14084  241 WKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
993-1240 5.45e-42

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: 154.80  E-value: 5.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd14184    9 IGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhlIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-DLRIPVPRVKLIDLEDAVQISGhfHIHHLLGNPEF 1149
Cdd:cd14184   89 AITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVcEYPDGTKSLKLGDFGLATVVEG--PLYTVCGTPTY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1150 AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDES--KEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFR 1227
Cdd:cd14184  167 VAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSPYWDNITDSAKELISHMLQVNVE 246
                        250
                 ....*....|...
gi 68362740 1228 RRPTAATCLQHPW 1240
Cdd:cd14184  247 ARYTAEQILSHPW 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
993-1240 9.93e-42

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: 153.83  E-value: 9.93e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkKEIIKRKEVEHtlnERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHLLGNP 1147
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSD---GHIKLTDFGLAKElSSDGDRTYTFCGTP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQEDFR 1227
Cdd:cd05123  158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPE----YVSPEAKSLISGLLQKDPT 233
                        250
                 ....*....|....*.
gi 68362740 1228 RRPTA--ATCL-QHPW 1240
Cdd:cd05123  234 KRLGSggAEEIkAHPF 249
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
987-1241 1.41e-41

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: 153.48  E-value: 1.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQreklKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISghfHIHH 1142
Cdd:cd14099   83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENM---NVKIGDFGLAARLE---YDGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 ----LLGNPEFAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfCGVSNAARDF 1217
Cdd:cd14099  157 rkktLCGTPNYIAPEVLEKKKGhSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSH--LSISDEAKDL 234
                        250       260
                 ....*....|....*....|....
gi 68362740 1218 INVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14099  235 IRSMLQPDPTKRPSLDEILSHPFF 258
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
993-1240 3.24e-41

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: 152.57  E-value: 3.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDdGRLL 1069
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQlrnEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH-GDML 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHD--ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNP 1147
Cdd:cd14082   90 EMILSSEkgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVGTP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFldesKEETCIN--VCRVDFSFPHEYFCGVSNAARDFINVILQED 1225
Cdd:cd14082  170 AYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF----NEDEDINdqIQNAAFMYPPNPWKEISPDAIDLINNLLQVK 245
                        250
                 ....*....|....*
gi 68362740 1226 FRRRPTAATCLQHPW 1240
Cdd:cd14082  246 MRKRYSVDKSLSHPW 260
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
993-1241 5.15e-41

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: 153.22  E-value: 5.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA-AHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14166   11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSlENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----DLRIPVPRVKLIDLEDavqisgHFHIHHLLGN 1146
Cdd:cd14166   91 ILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpdeNSKIMITDFGLSKMEQ------NGIMSTACGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDF 1226
Cdd:cd14166  165 PGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHLLEKNP 244
                        250
                 ....*....|....*
gi 68362740 1227 RRRPTAATCLQHPWL 1241
Cdd:cd14166  245 SKRYTCEKALSHPWI 259
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
993-1240 8.13e-41

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: 151.64  E-value: 8.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd14185    8 IGDGNFAVVKECRHWNENQEYAMKIIdkSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPR-VKLIDLEDAVQISGhfHIHHLLGNPEF 1149
Cdd:cd14185   88 AIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTtLKLADFGLAKYVTG--PIFTVCGTPTY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1150 AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLD-ESKEETCINVCRV-DFSFPHEYFCGVSNAARDFINVILQEDFR 1227
Cdd:cd14185  166 VAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQLgHYEFLPPYWDNISEAAKDLISRLLVVDPE 245
                        250
                 ....*....|...
gi 68362740 1228 RRPTAATCLQHPW 1240
Cdd:cd14185  246 KRYTAKQVLQHPW 258
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
983-1241 1.25e-40

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: 153.64  E-value: 1.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHeaALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14176   17 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE--ILLRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQISGHfhiH 1141
Cdd:cd14176   95 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAE---N 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNP----EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL---DESKEETCINVCRVDFSFPHEYFCGVSNAA 1214
Cdd:cd14176  172 GLLMTPcytaNFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTA 251
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14176  252 KDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
987-1241 1.36e-40

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: 152.10  E-value: 1.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHeaALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIE--ILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQISGHfhiHHLLG 1145
Cdd:cd14175   81 ELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNPESLRICDFGFAKQLRAE---NGLLM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NP----EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF---LDESKEETCINVCRVDFSFPHEYFCGVSNAARDFI 1218
Cdd:cd14175  158 TPcytaNFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLV 237
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14175  238 SKMLHVDPHQRLTAKQVLQHPWI 260
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
993-1241 3.26e-40

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: 149.59  E-value: 3.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd06606    8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEaleREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLID------LEDAVQISGhfhIHHL 1143
Cdd:cd06606   88 SLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVD---SDGVVKLADfgcakrLAEIATGEG---TKSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFldESKEETCINVCRVDFS-----FPheyfCGVSNAARDFI 1218
Cdd:cd06606  162 RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW--SELGNPVAALFKIGSSgepppIP----EHLSEEAKDFL 235
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06606  236 RKCLQRDPKKRPTADELLQHPFL 258
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
992-1240 2.07e-39

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: 148.13  E-value: 2.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05581    8 PLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKyvtiEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLID----------------LEDA 1131
Cdd:cd05581   88 LLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDM---HIKITDfgtakvlgpdsspestKGDA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 VQISGHFHIHH--LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcG 1209
Cdd:cd05581  165 DSQIAYNQARAasFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE----N 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 68362740 1210 VSNAARDFINVILQEDFRRRPTAATC------LQHPW 1240
Cdd:cd05581  241 FPPDAKDLIQKLLVLDPSKRLGVNENggydelKAHPF 277
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
993-1241 8.35e-39

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: 145.49  E-value: 8.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS----KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14079   10 LGVGSFGKVKLAEHELTGHKVAVKILNrqkiKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGGEL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLID--LEDAVQiSGHFhIHHLLGN 1146
Cdd:cd14079   90 FDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNM---NVKIADfgLSNIMR-DGEF-LKTSCGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGiPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQE 1224
Cdd:cd14079  165 PNYAAPEVISG-KLYAGpeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSH----LSPGARDLIKRMLVV 239
                        250
                 ....*....|....*..
gi 68362740 1225 DFRRRPTAATCLQHPWL 1241
Cdd:cd14079  240 DPLKRITIPEIRQHPWF 256
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
993-1241 8.54e-39

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: 145.63  E-value: 8.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14074   11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHlfqEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLedavQISGHFHIHHLL---- 1144
Cdd:cd14074   91 DYIMKHENGLNEDLArKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDF----GFSNKFQPGEKLetsc 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQG----IPvslGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINV 1220
Cdd:cd14074  165 GSLAYSAPEILLGdeydAP---AVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAH----VSPECKDLIRR 237
                        250       260
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14074  238 MLIRDPKKRASLEEIENHPWL 258
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
983-1266 1.06e-38

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: 146.92  E-value: 1.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVK------FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSY 1056
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKivdvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMNHDE---LMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAV 1132
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADagfVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHH-LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDeSKEETCINVCRVDFSFPHEYFCGVS 1211
Cdd:cd14094  161 QLGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHIS 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1212 NAARDFINVILQEDFRRRPTAATCLQHPWLQPHNGSYSKIPL-DT-SRLACFIERRK 1266
Cdd:cd14094  240 ESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLpETvEQLRKFNARRK 296
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
986-1241 2.00e-38

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: 144.68  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd14110    4 TYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI---DLripvprVKLIDL-------EDAVQIS 1135
Cdd:cd14110   84 PELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIItekNL------LKIVDLgnaqpfnQGKVLMT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHFHIHhllgnPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYfCGVSNAAR 1215
Cdd:cd14110  158 DKKGDY-----VETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCY-AGLSGGAV 231
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1216 DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14110  232 NFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
991-1241 2.58e-38

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: 144.29  E-value: 2.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd06627    6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKsvmGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISG-HFHIHHLLGN 1146
Cdd:cd06627   86 LASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKD---GLVKLADFGVATKLNEvEKDENSVVGT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS-FPHeyfcGVSNAARDFINVILQED 1225
Cdd:cd06627  163 PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPpLPE----NISPELRDFLLQCFQKD 238
                        250
                 ....*....|....*.
gi 68362740 1226 FRRRPTAATCLQHPWL 1241
Cdd:cd06627  239 PTLRPSAKELLKHPWL 254
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
983-1241 2.71e-38

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: 145.54  E-value: 2.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHeaALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14178    1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIE--ILLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQISGHfhiH 1141
Cdd:cd14178   79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNPESIRICDFGFAKQLRAE---N 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNP----EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL---DESKEETCINVCRVDFSFPHEYFCGVSNAA 1214
Cdd:cd14178  156 GLLMTPcytaNFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDSISDAA 235
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14178  236 KDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
987-1241 7.50e-38

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: 142.91  E-value: 7.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNE-IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd14078    4 YYELHEtIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDlpRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHiHHL 1143
Cdd:cd14078   84 PGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLD---EDQNLKLIDFGLCAKPKGGMD-HHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 L---GNPEFAAPEVIQGIPVsLGT--DIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFI 1218
Cdd:cd14078  160 EtccGSPAYAAPELIQGKPY-IGSeaDVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPE----WLSPSSKLLL 234
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14078  235 DQMLQVDPKKRITVKELLNHPWV 257
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
993-1241 1.02e-37

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: 142.83  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd14183   14 IGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-DLRIPVPRVKLIDLEDAVQISGhfHIHHLLGNPEF 1149
Cdd:cd14183   94 AITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLATVVDG--PLYTVCGTPTY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1150 AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCI--NVCRVDFSFPHEYFCGVSNAARDFINVILQEDFR 1227
Cdd:cd14183  172 VAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLfdQILMGQVDFPSPYWDNVSDSAKELITMMLQVDVD 251
                        250
                 ....*....|....
gi 68362740 1228 RRPTAATCLQHPWL 1241
Cdd:cd14183  252 QRYSALQVLEHPWV 265
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
987-1242 1.03e-37

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: 142.35  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQIS-GHFHIHHLL 1144
Cdd:cd06614   82 SLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKD---GSVKLADFGFAAQLTkEKSKRNSVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE----TCINVCRvDFSFPHeyfcGVSNAARDFINV 1220
Cdd:cd06614  159 GTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRalflITTKGIP-PLKNPE----KWSPEFKDFLNK 233
                        250       260
                 ....*....|....*....|..
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06614  234 CLVKDPEKRPSAEELLQHPFLK 255
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
993-1242 1.49e-37

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: 142.75  E-value: 1.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK----------EQAAHEAALLQHLQ-HPQYITLHDTYESPTSYILILE 1061
Cdd:cd14182   11 LGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSfspeevqelrEATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHFHIH 1141
Cdd:cd14182   91 LMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM---NIKLTDFGFSCQLDPGEKLR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNPEFAAPEVIQ----------GIPVslgtDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVS 1211
Cdd:cd14182  168 EVCGTPGYLAPEIIEcsmddnhpgyGKEV----DMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDRS 243
                        250       260       270
                 ....*....|....*....|....*....|.
gi 68362740 1212 NAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14182  244 DTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
987-1241 1.74e-37

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: 141.94  E-value: 1.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKC--IHKATRKDVAVKFVSKKmkkkeQAA---------HEAALLQHLQHPQYITLHDTYESPTS 1055
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKK-----KAPkdflekflpRELEILRKLRHPNIIQVYSIFERGSK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQIS 1135
Cdd:cd14080   77 VFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNN---NVKLSDFGFARLCP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHfHIHHL----LGNPEFAAPEVIQGIPVS-LGTDIWSIGVLTYVMLSGVSPFlDES--KEETCINVCRvDFSFPHEYFc 1208
Cdd:cd14080  154 DD-DGDVLsktfCGSAAYAAPEILQGIPYDpKKYDIWSLGVILYIMLCGSMPF-DDSniKKMLKDQQNR-KVRFPSSVK- 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 68362740 1209 GVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14080  230 KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
981-1241 2.13e-37

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: 142.42  E-value: 2.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKF--VSKKMKKKEQ-------AAHEAALLQHLQ-HPQYITLHDTY 1050
Cdd:cd14181    6 KEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIieVTAERLSPEQleevrssTLKEIHILRQVSgHPSIITLIDSY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1051 ESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLED 1130
Cdd:cd14181   86 ESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQL---HIKLSDFGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGHFHIHHLLGNPEFAAPEVIQ----------GIPVslgtDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF 1200
Cdd:cd14181  163 SCHLEPGEKLRELCGTPGYLAPEILKcsmdethpgyGKEV----DLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRY 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1201 SFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14181  239 QFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
990-1242 6.16e-37

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: 140.42  E-value: 6.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKF--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd06623    6 VKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDyLMNHDELMEEKVAFYI-RDIMEALQYLHNCR-VAHLDIKPENLLIDLRipvPRVKLID------LEDAVQISGHFh 1139
Cdd:cd06623   86 LAD-LLKKVGKIPEPVLAYIaRQILKGLDYLHTKRhIIHRDIKPSNLLINSK---GEVKIADfgiskvLENTLDQCNTF- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 ihhlLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLD---ESKEETCINVCRVD-FSFPHEYFcgvSNAAR 1215
Cdd:cd06623  161 ----VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPpgqPSFFELMQAICDGPpPSLPAEEF---SPEFR 233
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1216 DFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06623  234 DFISACLQKDPKKRPSAAELLQHPFIK 260
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
979-1241 1.81e-36

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: 140.57  E-value: 1.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  979 WK---ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESP 1053
Cdd:cd14168    1 WKkqvEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSieNEIAVLRKIKHENIVALEDIYESP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----DLRIPVPRVKLIDL 1128
Cdd:cd14168   81 NHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqdeESKIMISDFGLSKM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQIsghfhIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFC 1208
Cdd:cd14168  161 EGKGDV-----MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWD 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 68362740 1209 GVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14168  236 DISDSAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
993-1240 3.01e-36

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: 139.47  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSkkmkkkEQAAH-------EAALLQHLQ-HPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd14090   10 LGEGAYASVQTCINLYTGKEYAVKIIE------KHPGHsrsrvfrEVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIH--- 1141
Cdd:cd14090   84 GGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIKLSSTSMtpv 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 ---HLL---GNPEFAAPEVI-----QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKE-------ETCiNVCRV----- 1198
Cdd:cd14090  164 ttpELLtpvGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEdcgwdrgEAC-QDCQEllfhs 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 68362740 1199 ----DFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd14090  243 iqegEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
983-1241 3.88e-36

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: 139.38  E-value: 3.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHeaALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14177    2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIE--ILMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQISGHfhiH 1141
Cdd:cd14177   80 MKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANADSIRICDFGFAKQLRGE---N 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNP----EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL---DESKEETCINVCRVDFSFPHEYFCGVSNAA 1214
Cdd:cd14177  157 GLLLTPcytaNFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVSDAA 236
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14177  237 KDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
987-1241 9.21e-36

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: 137.95  E-value: 9.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIH-KATRKDVAVKFV-----SKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYI 1057
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAIKVVrkadlSSDNLKGSSRANilkEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIP-----VPRVKLIDLEDAV 1132
Cdd:cd14096   83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFE-PIPfipsiVKLRKADDDETKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 Q----ISG------------HFHIHHLL---------GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDES 1187
Cdd:cd14096  162 DegefIPGvggggigivklaDFGLSKQVwdsntktpcGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDES 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1188 KEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14096  242 IETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
987-1241 1.14e-35

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: 136.21  E-value: 1.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL----QHPQYITLHDTYESPTS--YILIL 1060
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGGnhLCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGrLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQISGHFH 1139
Cdd:cd05118   81 ELMGMN-LYELIkDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQ--LKLADFGLARSFTSPPY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IhHLLGNPEFAAPEVI-QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVdfsfpheyfCGvSNAARDFI 1218
Cdd:cd05118  158 T-PYVATRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRL---------LG-TPEALDLL 226
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd05118  227 SKMLKYDPAKRITASQALAHPYF 249
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
987-1241 1.83e-35

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: 136.12  E-value: 1.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKD--VAVKfVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYE-SPTSYILILELM 1063
Cdd:cd14112    5 FSFGSEIFRGRFSVIVKAVDSTTETDahCAVK-IFEVSDEASEAVREFESLRTLQHENVQRLIAAFKpSNFAYLVMEKLQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDgrLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHFHIHHl 1143
Cdd:cd14112   84 ED--VFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSW-QVKLVDFGRAQKVSKLGKVPV- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDE--SKEETCINVCRVDFSfPHEYFCGVSNAARDFINV 1220
Cdd:cd14112  160 DGDTDWASPEFHNPeTPITVQSDIWGLGVLTFCLLSGFHPFTSEydDEEETKENVIFVKCR-PNLIFVEATQEALRFATW 238
                        250       260
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14112  239 ALKKSPTRRMRTDEALEHRWL 259
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
987-1241 2.15e-35

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: 136.14  E-value: 2.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREkagSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLI----DLEDAVQISG--H 1137
Cdd:cd14097   83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNDKLNikvtDFGLSVQKYGlgE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDF 1217
Cdd:cd14097  163 DMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAAKNV 242
                        250       260
                 ....*....|....*....|....
gi 68362740 1218 INVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14097  243 LQQLLKVDPAHRMTASELLDNPWI 266
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
993-1255 4.39e-35

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: 136.71  E-value: 4.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQaaHEAALLQHLQ-HPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ--REIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGGELLER 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLedavqisGHFHI----HHLLGNP 1147
Cdd:cd14179   93 IKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDF-------GFARLkppdNQPLKTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 ----EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV-------DFSFPHEYFCGVSNAARD 1216
Cdd:cd14179  166 cftlHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEImkkikqgDFSFEGEAWKNVSQEAKD 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 68362740 1217 FINVILQEDFRRRPTAATCLQHPWLQphNGS-YSKIPLDT 1255
Cdd:cd14179  246 LIQGLLTVDPNKRIKMSGLRYNEWLQ--DGSqLSSNPLMT 283
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
993-1241 3.13e-34

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: 133.61  E-value: 3.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAHEAALLQHLQ-HPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd14173   10 LGEGAYARVQTCINLITNKEYAVKIIEKRPgHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSILS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKL--IDLEDAVQISGH---FHIHHLL- 1144
Cdd:cd14173   90 HIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKIcdFDLGSGIKLNSDcspISTPELLt 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 --GNPEFAAPEVIQGIPVSLGT-----DIWSIGVLTYVMLSGVSPFLDE-------SKEETC--------INVCRVDFSF 1202
Cdd:cd14173  170 pcGSAEYMAPEVVEAFNEEASIydkrcDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEACpacqnmlfESIQEGKYEF 249
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 68362740 1203 PHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14173  250 PEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
993-1240 5.45e-34

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: 131.76  E-value: 5.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKK----KEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14663    8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVAregmVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLR--IPVPRVKLIDLEDAVQISGhfHIHHLLGN 1146
Cdd:cd14663   88 FSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDgnLKISDFGLSALSEQFRQDG--LLHTTCGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQ-----GIPvslgTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPhEYFcgvSNAARDFINVI 1221
Cdd:cd14663  166 PNYVAPEVLArrgydGAK----ADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYP-RWF---SPGAKSLIKRI 237
                        250
                 ....*....|....*....
gi 68362740 1222 LQEDFRRRPTAATCLQHPW 1240
Cdd:cd14663  238 LDPNPSTRITVEQIMASPW 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
993-1241 5.71e-34

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: 131.91  E-value: 5.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS-----------KKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTS-- 1055
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkrregkNDRGKIKNAlddvRREIAIMKKLDHPNIVRLYEVIDDPESdk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 -YiLILELMDDGRLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL---- 1128
Cdd:cd14008   81 lY-LVLEYCEGGPVMELDSGDrvPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTAD---GTVKISDFgvse 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 -----EDAVQISghfhihhlLGNPEFAAPEVIQGIPVSL---GTDIWSIGVLTYVMLSGVSPFLDESKEETC--INVCRV 1198
Cdd:cd14008  157 mfedgNDTLQKT--------AGTPAFLAPELCDGDSKTYsgkAADIWALGVTLYCLVFGRLPFNGDNILELYeaIQNQND 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1199 DFSFPHEyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14008  229 EFPIPPE----LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
993-1241 1.43e-33

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: 131.18  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS----KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKkrdmIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID----------------LEDAV 1132
Cdd:cd05579   81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN---GHLKLTDfglskvglvrrqiklsIQKKS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfCGVSN 1212
Cdd:cd05579  158 NGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPED--PEVSD 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1213 AARDFINVILQEDFRRRP---TAATCLQHPWL 1241
Cdd:cd05579  236 EAKDLISKLLTPDPEKRLgakGIEEIKNHPFF 267
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
993-1241 3.05e-33

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: 129.73  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYI-LILELMDDGR 1067
Cdd:cd14163    8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQrflpRELQIVERLDHKNIIHVYEMLESADGKIyLVMELAEDGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvpRVKLIDLEDAVQI-SGHFHIHHLL-G 1145
Cdd:cd14163   88 VFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF----TLKLTDFGFAKQLpKGGRELSQTFcG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGVSPFlDESKEETCINVCRVDFSFPHEYfcGVSNAARDFINVILQE 1224
Cdd:cd14163  164 STAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF-DDTDIPKMLCQQQKGVSLPGHL--GVSRTCQDLLKRLLEP 240
                        250
                 ....*....|....*..
gi 68362740 1225 DFRRRPTAATCLQHPWL 1241
Cdd:cd14163  241 DMVLRPSIEEVSWHPWL 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
993-1241 4.75e-33

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: 128.95  E-value: 4.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14162    8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQkflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDL----EDAVQISGHFHIHHLL 1144
Cdd:cd14162   88 LDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNN---NLKITDFgfarGVMKTKDGKPKLSETY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 -GNPEFAAPEVIQGIPVS-LGTDIWSIGVLTYVMLSGVSPFlDESKEETCIN--VCRVDFSFPHEyfcgVSNAARDFINV 1220
Cdd:cd14162  165 cGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLKqvQRRVVFPKNPT----VSEECKDLILR 239
                        250       260
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFrRRPTAATCLQHPWL 1241
Cdd:cd14162  240 MLSPVK-KRITIEEIKRDPWF 259
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
993-1242 6.59e-33

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: 128.88  E-value: 6.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHiVQTRQQEHifsEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLLGNPE 1148
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSN---GYVKLVDFGFAKKLGSGRKTWTFCGTPE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 FAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF--LDESKEETCINVcrVDFSFPHEYFCGVSNAARDFINVILqedf 1226
Cdd:cd05572  158 YVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFggDDEDPMKIYNII--LKGIDKIEFPKYIDKNAKNLIKQLL---- 231
                        250       260
                 ....*....|....*....|....*
gi 68362740 1227 RRRPT---------AATCLQHPWLQ 1242
Cdd:cd05572  232 RRNPEerlgylkggIRDIKKHKWFE 256
SH3_Kalirin_2 cd11853
Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
628-686 2.25e-32

Second Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212787  Cd Length: 59  Bit Score: 119.85  E-value: 2.25e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68362740  628 SMAVIKDYYALKENEICVSQGEVVQVLAVNQQNMCLVYQPASDHSPAAEGWVPGSILAP 686
Cdd:cd11853    1 TMPVIQDYYALKEDEICVSQGEVVQILAANQQNMFLVYRPATDQSPAAEGWIPGSVLGH 59
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
981-1241 3.48e-32

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: 126.61  E-value: 3.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAytelNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSY 1056
Cdd:cd14116    5 EDFEIG----RPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHqlrrEVEIQSHLRHPNILRLYGYFHDATRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISG 1136
Cdd:cd14116   81 YLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG---SAGELKIADFGWSVHAPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHiHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARD 1216
Cdd:cd14116  158 SRR-TTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDF----VTEGARD 232
                        250       260
                 ....*....|....*....|....*
gi 68362740 1217 FINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14116  233 LISRLLKHNPSQRPMLREVLEHPWI 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
993-1241 4.65e-32

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: 126.41  E-value: 4.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----------------EAALLQHLQHPQYITLHDTYESPTSY 1056
Cdd:cd14077    9 IGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKERekrlekeisrdirtirEAALSSLLNHPHICRLRDFLRTPNHY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISG 1136
Cdd:cd14077   89 YMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS---KSGNIKIIDFGLSNLYDP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHLLGNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAAR 1215
Cdd:cd14077  166 RRLLRTFCGSLYFAAPELLQAQPyTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSY----LSSECK 241
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1216 DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14077  242 SLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
987-1241 6.18e-32

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: 125.91  E-value: 6.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcpENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLmNHDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISghfH--- 1139
Cdd:cd14069   83 SGGELFDKI-EPDVGMPEDVAqFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEN---DNLKISDFGLATVFR---Ykgk 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 ---IHHLLGNPEFAAPEVIQ-----GIPVslgtDIWSIGVLTYVMLSGVSPFlDESKeETCINVCrvDFSFPHE-YFC-- 1208
Cdd:cd14069  156 erlLNKMCGTLPYVAPELLAkkkyrAEPV----DVWSCGIVLFAMLAGELPW-DQPS-DSCQEYS--DWKENKKtYLTpw 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 68362740 1209 -GVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14069  228 kKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
1028-1241 6.63e-32

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: 125.91  E-value: 6.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1028 AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDI 1107
Cdd:cd14088   46 AKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1108 KPENLLIDLRIPVPRVKLIDLEDAVQISGhfHIHHLLGNPEFAAPEVI----QGIPVslgtDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14088  126 KLENLVYYNRLKNSKIVISDFHLAKLENG--LIKEPCGTPEYLAPEVVgrqrYGRPV----DCWAIGVIMYILLSGNPPF 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1184 LDESKEETCIN--------VCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14088  200 YDEAEEDDYENhdknlfrkILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
987-1241 1.31e-31

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: 124.81  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE------------QAAHEAALLQHLQHPQYITLHDTYESPT 1054
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDtwvrdrklgtvpLEIHILDTLNKRSHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 SYILILELMDDG-RLLDYLMNHdELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAV 1132
Cdd:cd14004   82 FYYLVMEKHGSGmDLFDFIERK-PNMDEKEAKYIfRQVADAVKHLHDQGIVHRDIKDENVILDGNG---TIKLIDFGSAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QI-SGHFHIhhLLGNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDesKEETCINVCRVDFSfpheyfcgV 1210
Cdd:cd14004  158 YIkSGPFDT--FVGTIDYAAPEVLRGNPyGGKEQDIWALGVLLYTLVFKENPFYN--IEEILEADLRIPYA--------V 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 68362740 1211 SNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14004  226 SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
990-1240 1.44e-31

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: 125.77  E-value: 1.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05580    6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiIKLKQVEHvlnEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGhfHIHHLLG 1145
Cdd:cd05580   86 GELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSD---GHIKITDFGFAKRVKD--RTYTLCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYfcgvSNAARDFINVILQED 1225
Cdd:cd05580  161 TPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFF----DPDAKDLIKRLLVVD 236
                        250       260
                 ....*....|....*....|
gi 68362740 1226 FRRR-----PTAATCLQHPW 1240
Cdd:cd05580  237 LTKRlgnlkNGVEDIKNHPW 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
993-1255 3.55e-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: 125.37  E-value: 3.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQaaHEAALLQHLQ-HPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQ--REVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGGELLDR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDA-VQISGHFHIHHLLGNPEFA 1150
Cdd:cd14180   92 IKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFArLRPQGSRPLQTPCFTLQYA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1151 APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCIN----VCRV---DFSFPHEYFCGVSNAARDFINVILQ 1223
Cdd:cd14180  172 APELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHaadiMHKIkegDFSLEGEAWKGVSEEAKDLVRGLLT 251
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1224 EDFRRRPTAATCLQHPWLQpHNGSYSKIPLDT 1255
Cdd:cd14180  252 VDPAKRLKLSELRESDWLQ-GGSALSSTPLMT 282
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
993-1242 7.39e-31

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: 123.60  E-value: 7.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSkkmkkkEQAAHEAA--------LLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKIIE------KNAGHSRSrvfrevetLYQCQGNKNILELIEFFEDDTRFYLVFEKLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKL--IDLEDAVQISGHF---- 1138
Cdd:cd14174   84 GGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKIcdFDLGSGVKLNSACtpit 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 --HIHHLLGNPEFAAPEVI-----QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDE-------SKEETCiNVCRVD----- 1199
Cdd:cd14174  164 tpELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwDRGEVC-RVCQNKlfesi 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1200 ----FSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14174  243 qegkYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
993-1240 1.21e-30

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: 124.70  E-value: 1.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05573    9 IGRGAFGEVWLVRDKDTGQVYAMKILRKSDMlKREQIAHvraERDILADADSPWIVRLHYAFQDEDHLYLVMEYMPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLID--------------------- 1127
Cdd:cd05573   89 MNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD---ADGHIKLADfglctkmnksgdresylndsv 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1128 ---LEDAVQISGHFHIHH------LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV--C 1196
Cdd:cd05573  166 ntlFQDNVLARRRPHKQRrvraysAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKImnW 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 68362740 1197 RVDFSFPHEYfcGVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd05573  246 KESLVFPDDP--DVSPEAIDLIRRLLCDPEDRLGSAEEIKAHPF 287
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
993-1245 1.97e-30

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: 121.90  E-value: 1.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14117   14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHqlrrEIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQiSGHFHIHHLLGNPE 1148
Cdd:cd14117   94 YKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYK---GELKIADFGWSVH-APSLRRRTMCGTLD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 FAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQEDFRR 1228
Cdd:cd14117  170 YLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPF----LSDGSRDLISKLLRYHPSE 245
                        250
                 ....*....|....*..
gi 68362740 1229 RPTAATCLQHPWLQPHN 1245
Cdd:cd14117  246 RLPLKGVMEHPWVKANS 262
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
987-1241 2.30e-30

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: 121.19  E-value: 2.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKK-------KEQAAHEAALL---QHLQHPQYITLHDTYESPTSY 1056
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTewamingPVPVPLEIALLlkaSKPGVPGVIRLLDWYERPDGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILE----LMDdgrLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipVPRVKLID----- 1127
Cdd:cd14005   82 LLIMErpepCQD---LFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLR--TGEVKLIDfgcga 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1128 -LEDAVQISghFHihhllGNPEFAAPEVIQ-----GIPVSlgtdIWSIGVLTYVMLSGVSPFldESKEEtcinVCRVDFS 1201
Cdd:cd14005  157 lLKDSVYTD--FD-----GTRVYSPPEWIRhgryhGRPAT----VWSLGILLYDMLCGDIPF--ENDEQ----ILRGNVL 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 68362740 1202 FPHeyfcGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14005  220 FRP----RLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
993-1240 2.57e-30

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: 120.79  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKklnKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEF 1149
Cdd:cd14009   81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAETLCGSPLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1150 AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRR 1229
Cdd:cd14009  161 MAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAER 240
                        250
                 ....*....|.
gi 68362740 1230 PTAATCLQHPW 1240
Cdd:cd14009  241 ISFEEFFAHPF 251
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
993-1241 3.11e-30

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: 120.97  E-value: 3.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS------KKMKKKEQAAHEAALLQHLQHP---QYITlhDTYESPTSYILiLELM 1063
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKEVSlvdddkKSRESVKQLEQEIALLSKLRHPnivQYYG--TEREEDNLYIF-LEYV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIHHL 1143
Cdd:cd06632   85 PGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVD---TNGVVKLADFGMAKHVEAFSFAKSF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVI--QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP---HeyfcgVSNAARDFI 1218
Cdd:cd06632  162 KGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPipdH-----LSPDAKDFI 236
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06632  237 RLCLQRDPEDRPTASQLLEHPFV 259
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
993-1241 3.46e-30

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: 121.80  E-value: 3.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVskkmKKKEQAAHEAALlqHLQ---HPQYITLHDTY---------ESPTSYILI- 1059
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL----LDRPKARTEVRL--HMMcsgHPNIVQIYDVYansvqfpgeSSPRARLLIv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFH 1139
Cdd:cd14171   88 MELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGFAKVDQGDLM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLlgNPEFAAPEVIQG-----------IPVSL------GTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR----- 1197
Cdd:cd14171  168 TPQF--TPYYVAPQVLEAqrrhrkersgiPTSPTpytydkSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDMKrkimt 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 68362740 1198 VDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14171  246 GSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
987-1241 6.56e-30

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: 119.80  E-value: 6.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ-AAH---EAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQdMVRirrEIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLedavQISGHFHIHH 1142
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNG---NAKIADF----GLSNLYSKDK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LL----GNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgvSNAARDF 1217
Cdd:cd14073  156 LLqtfcGSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQ-----PSDASGL 230
                        250       260
                 ....*....|....*....|....
gi 68362740 1218 INVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14073  231 IRWMLTVNPKRRATIEDIANHWWV 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
987-1242 1.38e-29

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: 119.82  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14209    3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVvKLKQVEHtlnEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGhfHIHH 1142
Cdd:cd14209   83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ---GYIKVTDFGFAKRVKG--RTWT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPhEYFcgvSNAARDFINVIL 1222
Cdd:cd14209  158 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP-SHF---SSDLKDLLRNLL 233
                        250       260
                 ....*....|....*....|....*
gi 68362740 1223 QEDFRRR-----PTAATCLQHPWLQ 1242
Cdd:cd14209  234 QVDLTKRfgnlkNGVNDIKNHKWFA 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
987-1237 1.84e-29

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: 118.91  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKArqdcLKEIDLLQQLNHPNIIKYLASFIENNELNIVLEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDG---RLLDYLMNHDELMEEKVAF-YIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGH- 1137
Cdd:cd08224   82 ADAGdlsRLIKHFKKQKRLIPERTIWkYFVQLCSALEHMHSKRIMHRDIKPANVFITAN---GVVKLGDLGLGRFFSSKt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKE--ETCINVCRVDFS-FPHEYFcgvSNAA 1214
Cdd:cd08224  159 TAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPpLPADLY---SQEL 235
                        250       260
                 ....*....|....*....|...
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQ 1237
Cdd:cd08224  236 RDLVAACIQPDPEKRPDISYVLD 258
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
993-1241 2.26e-29

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: 118.26  E-value: 2.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14071    8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKkiyREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLedavQISGHFHIHHLL----G 1145
Cdd:cd14071   88 DYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANM---NIKIADF----GFSNFFKPGELLktwcG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGiPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPheYFcgVSNAARDFINVILQ 1223
Cdd:cd14071  161 SPPYAAPEVFEG-KEYEGpqLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIP--FF--MSTDCEHLIRRMLV 235
                        250
                 ....*....|....*...
gi 68362740 1224 EDFRRRPTAATCLQHPWL 1241
Cdd:cd14071  236 LDPSKRLTIEQIKKHKWM 253
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
987-1239 2.80e-29

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: 117.95  E-value: 2.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK--FVSKKMKKKEQAAH-EAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKeiDLSNMSEKEREEALnEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYL----MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LEDAVQ 1133
Cdd:cd08215   82 DGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKD---GVVKLGDfgiskvLESTTD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 isghfHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFcgvSNA 1213
Cdd:cd08215  159 -----LAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQY---SSE 230
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd08215  231 LRDLVNSMLQKDPEKRPSANEILSSP 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
987-1241 3.35e-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: 3.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKfVSKKMKKKE----QAAHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK-KIRLDNEEEgipsTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MD-DgrLLDYLMNHDELMEEK-VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHF 1138
Cdd:cd07829   80 CDqD--LKKYLDKRPGPLPPNlIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRD---GVLKLADfgLARAFGIPLRT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHhllgnpEFA-----APEVIQGIPV-SLGTDIWSIGVLTYVMLSGVSPFLDESK---------------EETCINVCR 1197
Cdd:cd07829  155 YTH------EVVtlwyrAPEILLGSKHySTAVDIWSVGCIFAELITGKPLFPGDSEidqlfkifqilgtptEESWPGVTK 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1198 V---DFSFP-------HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07829  229 LpdyKPTFPkwpkndlEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
993-1229 5.60e-29

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: 118.01  E-value: 5.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetmALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd05577   81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLD---DHGHVRISDLGLAVEFKGGKKIKGRVGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQ-GIPVSLGTDIWSIGVLTYVMLSGVSPFLDE----SKEETCINVCRVDFSFPHEYfcgvSNAARDFINVI 1221
Cdd:cd05577  158 HGYMAPEVLQkEVAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYPDSF----SPEARSLCEGL 233

                 ....*...
gi 68362740 1222 LQEDFRRR 1229
Cdd:cd05577  234 LQKDPERR 241
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
987-1267 6.14e-29

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: 117.73  E-value: 6.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS--KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DlripvprVKLIDLEDAVQISGHF-H 1139
Cdd:cd06609   83 GGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLseegD-------VKLADFGVSGQLTSTMsK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDFSFP---------HEYfcgv 1210
Cdd:cd06609  155 RNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSD-------LHPMRVLFLIPknnppslegNKF---- 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1211 SNAARDFINVILQEDFRRRPTAATCLQHPWLqphnGSYSKipldTSRLACFIERRKH 1267
Cdd:cd06609  224 SKPFKDFVELCLNKDPKERPSAKELLKHKFI----KKAKK----TSYLTLLIERIKK 272
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
987-1203 9.82e-29

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: 116.47  E-value: 9.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM---KKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnpSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHFHIHHL 1143
Cdd:cd14072   82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADM---NIKIADFGFSNEFTPGNKLDTF 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1144 LGNPEFAAPEVIQGIPVSlG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP 1203
Cdd:cd14072  159 CGSPPYAAPELFQGKKYD-GpeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIP 219
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
991-1229 1.49e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 118.00  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   991 NEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHvaqEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGhfHIHHLLGN 1146
Cdd:PTZ00263  104 ELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVPD--RTFTLCGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQEDF 1226
Cdd:PTZ00263  179 PEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN----WFDGRARDLVKGLLQTDH 254

                  ...
gi 68362740  1227 RRR 1229
Cdd:PTZ00263  255 TKR 257
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
990-1241 1.56e-28

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: 115.82  E-value: 1.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05578    5 LRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRnvlnELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLLG 1145
Cdd:cd05578   85 GDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQ---GHVHITDFNIATKLTDGTLATSTSG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFldESKEETCIN-VCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:cd05578  162 TKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPY--EIHSRTSIEeIRAKFETASVLYPAGWSEEAIDLINKLLER 239
                        250
                 ....*....|....*...
gi 68362740 1225 DFRRR-PTAATCLQHPWL 1241
Cdd:cd05578  240 DPQKRlGDLSDLKNHPYF 257
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
990-1242 9.49e-28

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: 115.41  E-value: 9.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05574    6 IKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKrvltEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYL--MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----------DL---------------- 1116
Cdd:cd05574   86 GELFRLLqkQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfDLskqssvtpppvrkslr 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1117 -RIPVPRVKLIDLEDAVQISGhFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV 1195
Cdd:cd05574  166 kGSRRSSVKSIEKETFVAEPS-ARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNI 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1196 CRVDFSFPHEYfcGVSNAARDFINVILQEDFRRR----PTAATCLQHPWLQ 1242
Cdd:cd05574  245 LKKELTFPESP--PVSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFR 293
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
987-1241 9.95e-28

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: 113.59  E-value: 9.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA---AHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQrllSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHL 1143
Cdd:cd14075   84 SGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN---NCVKVGDFGFSTHAKRGETLNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQ-----GIPVslgtDIWSIGVLTYVMLSGVSPFLDES--KEETCInvCRVDFSFPHEyfcgVSNAARD 1216
Cdd:cd14075  161 CGSPPYAAPELFKdehyiGIYV----DIWALGVLLYFMVTGVMPFRAETvaKLKKCI--LEGTYTIPSY----VSEPCQE 230
                        250       260
                 ....*....|....*....|....*
gi 68362740 1217 FINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14075  231 LIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
989-1241 1.30e-27

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: 113.13  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNE-IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKkEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd06612    6 DILEkLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDL-QEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDyLMN--HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISG-HFHIHHLL 1144
Cdd:cd06612   85 VSD-IMKitNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEE---GQAKLADFGVSGQLTDtMAKRNTVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDFSFPHEYFCGVSNAAR------DFI 1218
Cdd:cd06612  161 GTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSD-------IHPMRAIFMIPNKPPPTLSDPEKwspefnDFV 233
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06612  234 KKCLVKDPEERPSAIQLLQHPFI 256
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
993-1240 1.95e-27

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: 112.83  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH------EAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEvkalecEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLripVPRVKLIDLEDAVQ---ISGHFHIHHL 1143
Cdd:cd06625   88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDS---NGNVKLGDFGASKRlqtICSSTGMKSV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPHEyfcgVSNAARDFINVI 1221
Cdd:cd06625  165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAtqPTNPQLPPH----VSEDARDFLSLI 240
                        250
                 ....*....|....*....
gi 68362740 1222 LQEDFRRRPTAATCLQHPW 1240
Cdd:cd06625  241 FVRNKKQRPSAEELLSHSF 259
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
993-1241 2.42e-27

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: 112.60  E-value: 2.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE-----QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDsyvtkNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLID--LEDAVQISGHFH-IHHLL 1144
Cdd:cd14070   90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDEND---NIKLIDfgLSNCAGILGYSDpFSTQC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFpHEYFCGVSNAARDFINVILQE 1224
Cdd:cd14070  167 GSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEM-NPLPTDLSPGAISFLRSLLEP 245
                        250
                 ....*....|....*..
gi 68362740 1225 DFRRRPTAATCLQHPWL 1241
Cdd:cd14070  246 DPLKRPNIKQALANRWL 262
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
987-1240 3.29e-27

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: 112.00  E-value: 3.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd14665   82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGS-PAPRLKICDFGYSKSSVLHSQPKSTVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLG-TDIWSIGVLTYVMLSGVSPFLDESK----EETCINVCRVDFSFPHeyFCGVSNAARDFINVI 1221
Cdd:cd14665  161 PAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFEDPEEprnfRKTIQRILSVQYSIPD--YVHISPECRHLISRI 238
                        250
                 ....*....|....*....
gi 68362740 1222 LQEDFRRRPTAATCLQHPW 1240
Cdd:cd14665  239 FVADPATRITIPEIRNHEW 257
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
987-1241 4.14e-27

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: 111.57  E-value: 4.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd14002    3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRnlrQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DdGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHI-HH 1142
Cdd:cd14002   83 Q-GELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG---KGGVVKLCDFGFARAMSCNTLVlTS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVIL 1222
Cdd:cd14002  159 IKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSN----MSPEFKSFLQGLL 234
                        250
                 ....*....|....*....
gi 68362740 1223 QEDFRRRPTAATCLQHPWL 1241
Cdd:cd14002  235 NKDPSKRLSWPDLLEHPFV 253
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
992-1241 5.22e-27

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: 111.55  E-value: 5.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVA---VKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP--TSYILILELMDDG 1066
Cdd:cd13983    8 VLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKskKEVIFITELMTSG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR--VAHLDIKPENLLIDlrIPVPRVKLIDLEDAVQISGHFhIHHLL 1144
Cdd:cd13983   88 TLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFIN--GNTGEVKIGDLGLATLLRQSF-AKSVI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGipvSLGT--DIWSIGVLTYVMLSGVSPFldeskeETCINVC----RVDFSFPHEYFCGVSN-AARDF 1217
Cdd:cd13983  165 GTPEFMAPEMYEE---HYDEkvDIYAFGMCLLEMATGEYPY------SECTNAAqiykKVTSGIKPESLSKVKDpELKDF 235
                        250       260
                 ....*....|....*....|....*
gi 68362740 1218 I-NVILQEDfrRRPTAATCLQHPWL 1241
Cdd:cd13983  236 IeKCLKPPD--ERPSARELLEHPFF 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
984-1242 5.81e-27

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: 112.02  E-value: 5.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIH-KATRKDVAVKFVSKKMKKKEQA--AHEAALLQHLQHPQYITLHDTYESPTSYILIL 1060
Cdd:cd14201    5 DFEYSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQIllGKEIKILKELQHENIVALYDVQEMPNSVFLVM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL------RIPVPRVKLIDLEDAVQI 1134
Cdd:cd14201   85 EYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYasrkksSVSGIRIKIADFGFARYL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1135 SGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR---VDFSFPHEyfcgVS 1211
Cdd:cd14201  165 QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKnknLQPSIPRE----TS 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 68362740 1212 NAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14201  241 PYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
987-1241 8.40e-27

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: 111.65  E-value: 8.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKK---KEQAAHEAALLQHLQHPQYIT-LHDTYESPTSYILILEL 1062
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEggiPNQALREIKALQACQGHPYVVkLRDVFPHGTGFVLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGrLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQIS--GHFH 1139
Cdd:cd07832   82 MLSS-LSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS---STGVLKIADFGLARLFSeeDPRL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESK-EETCInVCRV----------------DFS 1201
Cdd:cd07832  158 YSHQVATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNGSPLFPGENDiEQLAI-VLRTlgtpnektwpeltslpDYN 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740 1202 ---FPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07832  237 kitFPEskgirleEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
1001-1240 2.10e-26

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: 110.07  E-value: 2.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1001 VKKCIHKATRKDVAVKFVskkmKKKEQAAHEAALlqHL---QHPQYITLHDTYE---SPTSYILI-LELMDDGRLLDYLM 1073
Cdd:cd14089   17 VLECFHKKTGEKFALKVL----RDNPKARREVEL--HWrasGCPHIVRIIDVYEntyQGRKCLLVvMECMEGGELFSRIQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1074 NHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAA 1151
Cdd:cd14089   91 ERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQTPCYTPYYVA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1152 PEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLdeSKEETCIN------VCRVDFSFPHEYFCGVSNAARDFINVILQED 1225
Cdd:cd14089  171 PEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY--SNHGLAISpgmkkrIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTD 248
                        250
                 ....*....|....*
gi 68362740 1226 FRRRPTAATCLQHPW 1240
Cdd:cd14089  249 PSERLTIEEVMNHPW 263
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
987-1241 1.21e-25

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: 107.95  E-value: 1.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATR-----KDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYI 1057
Cdd:cd14076    3 YILGRTLGEGEFGKVKLGWPLPKAnhrsgVQVAIKLIRRDTQQENCQTskimREINILKGLTHPNIVRLLDVLKTKKYIG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlripvpRVKLIDLEDAVQISGH 1137
Cdd:cd14076   83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD------KNRNLVITDFGFANTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLL-----GNPEFAAPEVIQGIPVSLGT--DIWSIGVLTYVMLSGVSPFLDESKEETCINV-------CRVDFSFP 1203
Cdd:cd14076  157 DHFNGDLmstscGSPCYAAPELVVSDSMYAGRkaDIWSCGVILYAMLAGYLPFDDDPHNPNGDNVprlyryiCNTPLIFP 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 68362740 1204 hEYfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14076  237 -EY---VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
987-1183 1.80e-25

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: 106.96  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDSSGRL-VAIKSIRKDRIKDEQdllhIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH 1142
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDAN---GNIKIADFGLSNLYNQDKFLQT 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1143 LLGNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14161  161 YCGSPLYASPEIVNGRPyIGPEVDSWSLGVLLYILVHGTMPF 202
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
987-1240 1.86e-25

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: 107.16  E-value: 1.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd14662   82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGS-PAPRLKICDFGYSKSSVLHSQPKSTVGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSlG--TDIWSIGVLTYVMLSGVSPFLDESK----EETCINVCRVDFSFPHeyFCGVSNAARDFINV 1220
Cdd:cd14662  161 PAYIAPEVLSRKEYD-GkvADVWSCGVTLYVMLVGAYPFEDPDDpknfRKTIQRIMSVQYKIPD--YVRVSQDCRHLLSR 237
                        250       260
                 ....*....|....*....|
gi 68362740 1221 ILQEDFRRRPTAATCLQHPW 1240
Cdd:cd14662  238 IFVANPAKRITIPEIKNHPW 257
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
993-1242 2.11e-25

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: 107.02  E-value: 2.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRK-DVAVKFVSKKMKKKEQA--AHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14202   10 IGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQTllGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL---RIPVP---RVKLIDLEDAVQISGHFHIHHL 1143
Cdd:cd14202   90 DYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYsggRKSNPnniRIKIADFGFARYLQNNMMAATL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR---VDFSFPHEyfcgVSNAARDFINV 1220
Cdd:cd14202  170 CGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKnksLSPNIPRE----TSSHLRQLLLG 245
                        250       260
                 ....*....|....*....|..
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14202  246 LLQRNQKDRMDFDEFFHHPFLD 267
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
981-1242 3.69e-25

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: 108.09  E-value: 3.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSayteLNEIGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSY 1056
Cdd:cd05599    1 EDFEP----LKVIGRGAFGEVRLVRKKDTGHVYAMKKLrKSEMLEKEQVAHvraERDILAEADNPWVVKLYYSFQDEENL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLedavQISG 1136
Cdd:cd05599   77 YLIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR---GHIKLSDF----GLCT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHL----LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV--CRVDFSFPHEyfCGV 1210
Cdd:cd05599  150 GLKKSHLaystVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKImnWRETLVFPPE--VPI 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 68362740 1211 SNAARDFINVILQEDFRR--RPTAATCLQHPWLQ 1242
Cdd:cd05599  228 SPEAKDLIERLLCDAEHRlgANGVEEIKSHPFFK 261
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
988-1241 4.18e-25

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: 105.99  E-value: 4.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  988 TELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd06648   10 DNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDlRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF-HIHHLLG 1145
Cdd:cd06648   90 ALTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSD---GRVKLSDFGFCAQVSKEVpRRKSLVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVcRVD----FSFPHEyfcgVSNAARDFINVI 1221
Cdd:cd06648  166 TPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRI-RDNeppkLKNLHK----VSPRLRSFLDRM 240
                        250       260
                 ....*....|....*....|
gi 68362740 1222 LQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06648  241 LVRDPAQRATAAELLNHPFL 260
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
992-1240 4.62e-25

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: 106.22  E-value: 4.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKfvSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14010    7 EIGRGKHSVVYKGRRKGTIEFVAIK--CVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDL-------EDAVQISGHFHIHH-- 1142
Cdd:cd14010   85 LRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD---GNGTLKLSDFglarregEILKELFGQFSDEGnv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 --------LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP-HEYFCGVSNA 1213
Cdd:cd14010  162 nkvskkqaKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPpPKVSSKPSPD 241
                        250       260
                 ....*....|....*....|....*...
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHP-W 1240
Cdd:cd14010  242 FKSLLKGLLEKDPAKRLSWDELVKHPfW 269
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
996-1241 5.27e-25

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 106.09  E-value: 5.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   996 GRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAHEaaLLQHlqHPQYITLHDTYESPTSYILILELMDDGRLLDYLMN 1074
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAKNfNAIEPMVHQ--LMKD--NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1075 HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlrIPVPRVKLID--LedaVQISGHFHIHHllGNPEFAAP 1152
Cdd:PHA03390  103 EGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYD--RAKDRIYLCDygL---CKIIGTPSCYD--GTLDYFSP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1153 EVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRR-PT 1231
Cdd:PHA03390  176 EKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLPFIKNVSKNANDFVQSMLKYNINYRlTN 255
                         250
                  ....*....|
gi 68362740  1232 AATCLQHPWL 1241
Cdd:PHA03390  256 YNEIIKHPFL 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
993-1240 6.57e-25

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: 105.45  E-value: 6.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKA-TRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDtYESPTSYI-LILELMDDGR 1067
Cdd:cd14121    3 LGSGTYATVYKAYRKSgAREVVAVKCVsksSLNKASTENLLTEIELLKKLKHPHIVELKD-FQWDEEHIyLIMEYCSGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIPVPRVKLIDLEDAVQISGHFHIHHLLGNP 1147
Cdd:cd14121   82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLS-SRYNPVLKLADFGFAQHLKPNDEAHSLRGSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETcinVCRVDFSFPHEYFCG--VSNAARDFINVILQED 1225
Cdd:cd14121  161 LYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEEL---EEKIRSSKPIEIPTRpeLSADCRDLLLRLLQRD 237
                        250
                 ....*....|....*
gi 68362740 1226 FRRRPTAATCLQHPW 1240
Cdd:cd14121  238 PDRRISFEEFFAHPF 252
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
987-1241 7.05e-25

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: 105.43  E-value: 7.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLqhpqyitlhDTYESPTSYILIlelmddg 1066
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELL---------NKKDKADKYHIV------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLM--NH------------DELMEEKVAFY---------IRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRV 1123
Cdd:cd14133   65 RLKDVFYfkNHlcivfellsqnlYEFLKQNKFQYlslprirkiAQQILEALVFLHSLGLIHCDLKPENILL-ASYSRCQI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1124 KLIDLEDAVQISGhfHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP 1203
Cdd:cd14133  144 KIIDFGSSCFLTQ--RLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPP 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1204 hEYFCGVSNAAR----DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14133  222 -AHMLDQGKADDelfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
994-1240 8.06e-25

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: 107.11  E-value: 8.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  994 GRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--AAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05584    8 GYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQkdTAHtkaERNILEAVKHPFIVDLHYAFQTGGKLYLILEYLSGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL----EdavQISGHFHIHHLL 1144
Cdd:cd05584   88 FMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQ---GHVKLTDFglckE---SIHDGTVTHTFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeYfcgVSNAARDFINVILQE 1224
Cdd:cd05584  162 GTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPP-Y---LTNEARDLLKKLLKR 237
                        250       260
                 ....*....|....*....|.
gi 68362740 1225 DFRRR----PTAATCLQ-HPW 1240
Cdd:cd05584  238 NVSSRlgsgPGDAEEIKaHPF 258
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
993-1241 8.74e-25

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: 105.46  E-value: 8.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH--EAALLQHLQHpqyitLHDTYE----SPTSYILILELMDDG 1066
Cdd:cd14172   12 LGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHhwRASGGPHIVH-----ILDVYEnmhhGKRCLLIIMECMEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNH-DELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLL 1144
Cdd:cd14172   87 ELFSRIQERgDQAFTEREASEImRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQNALQTPC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV----DFSFPHEYFCGVSNAARDFINV 1220
Cdd:cd14172  167 YTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRirmgQYGFPNPEWAEVSEEAKQLIRH 246
                        250       260
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14172  247 LLKTDPTERMTITQFMNHPWI 267
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
985-1229 9.87e-25

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: 107.02  E-value: 9.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA-----AHEAALLQHLQHPQYITLHDTYESPTSYILI 1059
Cdd:cd05602    7 SDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEekhimSERNVLLKNVKHPFLVGLHFSFQTTDKLYFV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGhfH 1139
Cdd:cd05602   87 LDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNG--T 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVcrvdFSFPHEYFCGVSNAARDFIN 1219
Cdd:cd05602  165 TSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNI----LNKPLQLKPNITNSARHLLE 240
                        250
                 ....*....|
gi 68362740 1220 VILQEDFRRR 1229
Cdd:cd05602  241 GLLQKDRTKR 250
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
993-1229 1.33e-24

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: 105.60  E-value: 1.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMK---KKEQAAH-EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05612    9 IGTGTFGRVHLVRDRISEHYYALKVMAIPEVirlKQEQHVHnEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQIsgHFHIHHLLGNPE 1148
Cdd:cd05612   89 FSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKE---GHIKLTDFGFAKKL--RDRTWTLCGTPE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 FAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYfcgvSNAARDFINVILQEDFRR 1228
Cdd:cd05612  164 YLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHL----DLYAKDLIKKLLVVDRTR 239

                 .
gi 68362740 1229 R 1229
Cdd:cd05612  240 R 240
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
993-1241 1.70e-24

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: 104.31  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDV--AVKFV------SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS-YILILELM 1063
Cdd:cd13994    1 IGKGATSVVRIVTKKNPRSGVlyAVKEYrrrddeSKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHFH--IH 1141
Cdd:cd13994   81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG---VLKLTDFGTAEVFGMPAEkeSP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 H---LLGNPEFAAPEVIQGIPVS-LGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNA---- 1213
Cdd:cd13994  158 MsagLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPIENLlpse 237
                        250       260
                 ....*....|....*....|....*...
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd13994  238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
987-1241 1.88e-24

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: 104.17  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSkkmkkkEQAAHEAALLQ----------HLQHPQYITLHDTYESPTSY 1056
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMID------KKAMQKAGMVQrvrneveihcQLKHPSILELYNYFEDSNYV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQIS 1135
Cdd:cd14186   77 YLVLEMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNM---NIKIADFGLATQLK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHFHIHHLL-GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAA 1214
Cdd:cd14186  154 MPHEKHFTMcGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAF----LSREA 229
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14186  230 QDLIHQLLRKNPADRLSLSSVLDHPFM 256
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
953-1241 1.95e-24

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 106.45  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   953 ISLPSEPSEFVRLPEYDAAADGATISWKENFdSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAH 1030
Cdd:PLN00034   43 VPLPLPPPSSSSSSSSSSSASGSAPSAAKSL-SELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1031 EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHdelmEEKVAFYIRDIMEALQYLHNCRVAHLDIKPE 1110
Cdd:PLN00034  122 EIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIAD----EQFLADVARQILSGIAYLHRRHIVHRDIKPS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1111 NLLIDLRipvPRVKLIDledavqisghFHIHHLL-----------GNPEFAAPEVI-----QGIPVSLGTDIWSIGVLTY 1174
Cdd:PLN00034  198 NLLINSA---KNVKIAD----------FGVSRILaqtmdpcnssvGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSIL 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740  1175 VMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:PLN00034  265 EFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
985-1253 2.08e-24

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: 104.48  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA--AHEAALLQHLQHPQ---YITLHDTYESPTSYILI 1059
Cdd:cd06917    1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSdiQKEVALLSQLKLGQpknIIKYYGSYLKGPSLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI-SGHF 1138
Cdd:cd06917   81 MDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNT---GNVKLCDFGVAASLnQNSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHHLLGNPEFAAPEVI-QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVcrVDFSFPHEYFCGVSNAARDF 1217
Cdd:cd06917  157 KRSTFVGTPYWMAPEVItEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLI--PKSKPPRLEGNGYSPLLKEF 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 68362740 1218 INVILQEDFRRRPTAATCLQHPWLQphngSYSKIPL 1253
Cdd:cd06917  235 VAACLDEEPKDRLSADELLKSKWIK----QHSKTPT 266
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
984-1242 2.83e-24

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: 103.85  E-value: 2.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd06647    6 KKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH 1142
Cdd:cd06647   86 LAGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 -LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDFSFPHEyfcgVSNAARDFI 1218
Cdd:cd06647  162 tMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFL 237
                        250       260
                 ....*....|....*....|....
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06647  238 NRCLEMDVEKRGSAKELLQHPFLK 261
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
987-1239 2.91e-24

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: 103.63  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVnlgSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDE----LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI---DLripvprVKLIDLEDAVQISG 1136
Cdd:cd08530   82 PFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLsagDL------VKIGDLGISKVLKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFhIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFcgvsnaARD 1216
Cdd:cd08530  156 NL-AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVY------SQD 228
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1217 FINVI---LQEDFRRRPTAATCLQHP 1239
Cdd:cd08530  229 LQQIIrslLQVNPKKRPSCDKLLQSP 254
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
985-1241 3.09e-24

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: 103.71  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTElneigRGRFSIVKKCIH-KATRKDVAVKFVSkkmkkkeqaaHEAALLQHLQHPQYITLHDTYESPTSYILI-LEL 1062
Cdd:cd14165   19 SAYSE-----RLKCNVAIKIIDkKKAPDDFVEKFLP----------RELEILARLNHKSIIKTYEIFETSDGKVYIvMEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLID-------LEDA---V 1132
Cdd:cd14165   84 GVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDF---NIKLTDfgfskrcLRDEngrI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFhihhlLGNPEFAAPEVIQGIPVSLGT-DIWSIGVLTYVMLSGVSPFlDESKEETCINV---CRVDfsFPHEyfC 1208
Cdd:cd14165  161 VLSKTF-----CGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPY-DDSNVKKMLKIqkeHRVR--FPRS--K 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 68362740 1209 GVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14165  231 NLTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
990-1245 4.36e-24

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: 103.19  E-value: 4.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd06605    6 LGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALqkQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR-VAHLDIKPENLLIDLRipvPRVKLIDLedavQISGHFhIHHL--- 1143
Cdd:cd06605   86 LDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSR---GQVKLCDF----GVSGQL-VDSLakt 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 -LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFlDESKEETCINV-----CRVDFS---FPHEYFcgvSNAA 1214
Cdd:cd06605  158 fVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPY-PPPNAKPSMMIfellsYIVDEPpplLPSGKF---SPDF 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWLQPHN 1245
Cdd:cd06605  234 QDFVSQCLQKDPTERPSYKELMEHPFIKRYE 264
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1039-1258 5.23e-24

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: 103.96  E-value: 5.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1039 QHPQYITLHDTYE----SPTSYILILELMDDGRLLDYLMNH-DELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENL 1112
Cdd:cd14170   53 QCPHIVRIVDVYEnlyaGRKCLLIVMECLDGGELFSRIQDRgDQAFTEREASEImKSIGEAIQYLHSINIAHRDVKPENL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1113 LIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLdeSKEETC 1192
Cdd:cd14170  133 LYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY--SNHGLA 210
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1193 IN------VCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQpHNGSYSKIPLDTSRL 1258
Cdd:cd14170  211 ISpgmktrIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIM-QSTKVPQTPLHTSRV 281
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
986-1239 1.48e-23

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: 101.85  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVK---FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTY---ESPTSYIlI 1059
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKeidYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIvdrANTTLYI-V 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYLMNHDE----LMEEKVAFYIRDIMEALQYLHNC-----RVAHLDIKPENLLIDLRipvPRVKLIDLED 1130
Cdd:cd08217   80 MEYCEGGDLAQLIKKCKKenqyIPEEFIWKIFTQLLLALYECHNRsvgggKILHRDLKPANIFLDSD---NNVKLGDFGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGH-FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSF-PHEYfc 1208
Cdd:cd08217  157 ARVLSHDsSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRiPSRY-- 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 68362740 1209 gvSNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd08217  235 --SSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
992-1241 1.55e-23

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: 102.37  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVkkCI--HKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd06659   28 KIGEGSTGVV--CIarEKHSGRQVAVKMMDlRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHF-HIHHLLGNP 1147
Cdd:cd06659  106 TD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG---RVKLSDFGFCAQISKDVpKRKSLVGTP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETcinVCRVDFSFPHEY--FCGVSNAARDFINVILQED 1225
Cdd:cd06659  182 YWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQA---MKRLRDSPPPKLknSHKASPVLRDFLERMLVRD 258
                        250
                 ....*....|....*.
gi 68362740 1226 FRRRPTAATCLQHPWL 1241
Cdd:cd06659  259 PQERATAQELLDHPFL 274
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
992-1253 1.66e-23

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: 102.42  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd06658   29 KIGEGSTGIVCIATEKHTGKQVAVKKMDlRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 yLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLEDAVQISGHF-HIHHLLGNPEF 1149
Cdd:cd06658  109 -IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILL---TSDGRIKLSDFGFCAQVSKEVpKRKSLVGTPYW 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1150 AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETcinVCRVDFSFPHEY--FCGVSNAARDFINVILQEDFR 1227
Cdd:cd06658  185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQA---MRRIRDNLPPRVkdSHKVSSVLRGFLDLMLVREPS 261
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1228 RRPTAATCLQHPWLQPHNGSYSKIPL 1253
Cdd:cd06658  262 QRATAQELLQHPFLKLAGPPSCIVPL 287
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
993-1241 2.87e-23

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: 100.41  E-value: 2.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVK-----FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS---YIlILELMD 1064
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKilkkrKLRRIPNGEANVKREIQILRRLNHRNVIKLVDVLYNEEKqklYM-VMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 dGRLLDYLmnhDELMEEKVAF-----YIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISgHFH 1139
Cdd:cd14119   80 -GGLQEML---DSAPDKRLPIwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTD---GTLKISDFGVAEALD-LFA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 ----IHHLLGNPEFAAPEVIQGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNA 1213
Cdd:cd14119  152 eddtCTTSQGSPAFQPPEIANGQDSFSGfkVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDD----VDPD 227
                        250       260
                 ....*....|....*....|....*...
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14119  228 LQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
990-1240 3.44e-23

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: 100.63  E-value: 3.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA-----AHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQvtnvkAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHfhIHH 1142
Cdd:cd05611   81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT---GHLKLTDfgLSRNGLEKRH--NKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVIL 1222
Cdd:cd05611  156 FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLL 235
                        250       260
                 ....*....|....*....|.
gi 68362740 1223 QEDFRRRPTA---ATCLQHPW 1240
Cdd:cd05611  236 CMDPAKRLGAngyQEIKSHPF 256
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1026-1245 3.50e-23

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: 101.23  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1026 EQAAHEAALLQHL-QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAH 1104
Cdd:cd05613   49 EHTRTERQVLEHIrQSPFLVTLHYAFQTDTKLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1105 LDIKPENLLIDlriPVPRVKLIDLedavQISGHF------HIHHLLGNPEFAAPEVIQGIPV--SLGTDIWSIGVLTYVM 1176
Cdd:cd05613  129 RDIKLENILLD---SSGHVVLTDF----GLSKEFlldeneRAYSFCGTIEYMAPEIVRGGDSghDKAVDWWSLGVLMYEL 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1177 LSGVSPFL----DESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQEDFRRR----PTAATCL-QHPWLQPHN 1245
Cdd:cd05613  202 LTGASPFTvdgeKNSQAEISRRILKSEPPYPQE----MSALAKDIIQRLLMKDPKKRlgcgPNGADEIkKHPFFQKIN 275
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
993-1245 3.55e-23

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: 101.97  E-value: 3.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM--KKKEQA---AHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTilKKKEQNhimAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL---EDAVQISGhfHIHHLL 1144
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQ---GHVVLTDFglcKEGMEPEE--TTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQE 1224
Cdd:cd05603  158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPG----GKTVAACDLLQGLLHK 233
                        250       260
                 ....*....|....*....|....*
gi 68362740 1225 DFRRRPTAATCLQ----HPWLQPHN 1245
Cdd:cd05603  234 DQRRRLGAKADFLeiknHVFFSPIN 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
993-1241 4.67e-23

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: 100.30  E-value: 4.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----------EAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRkksmldalqrEIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LEDAVQISG 1136
Cdd:cd06628   88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNK---GGIKISDfgiskkLEANSLSTK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 -HFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV-CRVDFSFPHEyfcgVSNAA 1214
Cdd:cd06628  165 nNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIgENASPTIPSN----ISSEA 240
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1215 RDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06628  241 RDFLEKTFEIDHNKRPTADELLKHPFL 267
I-set pfam07679
Immunoglobulin I-set domain;
774-868 6.05e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 94.25  E-value: 6.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNIldtdNSSATYTVSsCDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPL----RSSDRFKVT-YEGGTYTLTISNVQPDDSGKYTCVA 75
                           90
                   ....*....|....*
gi 68362740    854 TNDHGTTSTSATVKV 868
Cdd:pfam07679   76 TNSAGEAEASAELTV 90
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
405-531 6.57e-23

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 95.82  E-value: 6.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  405 NDMMNLGRLQGFEGTLTAQGKLLQQDTFYVIeldagmQSRTK-ERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYL 483
Cdd:cd13242    8 NDLLAMDSIRGCDVNLKEQGQLLRQDEFLVW------QGRKKcLRHVFLFEDLILFSKPKKTPGGKDVYIYKHSIKTSDI 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740  484 VLEENVDNDPCKFAL--MNRETSERVVLQAANADIQQAWVQDINQVLETQ 531
Cdd:cd13242   82 GLTENVGDSGLKFEIwfRRRKARDTYILQATSPEIKQAWTSDIAKLLWKQ 131
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
992-1240 7.83e-23

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: 99.74  E-value: 7.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVS------------------------KKMKKKEQAAHEAALLQHLQHPQYITLH 1047
Cdd:cd14118    1 EIGKGSYGIVKLAYNEEDNTLYAMKILSkkkllkqagffrrppprrkpgalgKPLDPLDRVYREIAILKKLDHPNVVKLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1048 DTYESPT--SYILILELMDDGRLLDylMNHDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVK 1124
Cdd:cd14118   81 EVLDDPNedNLYMVFELVDKGAVME--VPTDNPLSEETArSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG---DDGHVK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1125 LIDLedavQISGHFH-IHHLL----GNPEFAAPEVIQGIPVSLG---TDIWSIGVLTYVMLSGVSPFLDESKEETCINVC 1196
Cdd:cd14118  156 IADF----GVSNEFEgDDALLsstaGTPAFMAPEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIK 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 68362740 1197 RVDFSFPHEyfCGVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd14118  232 TDPVVFPDD--PVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
991-1241 8.37e-23

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: 99.68  E-value: 8.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVKKCIHKATRKDVAVK---FVSKKMKKKEQAAHEAALLQHLQHP---QY--ITLHdtyeSPTSYILiLEL 1062
Cdd:cd06626    6 NKIGEGTFGKVYTAVNLDTGELMAMKeirFQDNDPKTIKEIADEMKVLEGLDHPnlvRYygVEVH----REEVYIF-MEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPvprVKLIDLEDAVQIS------G 1136
Cdd:cd06626   81 CQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL---IKLGDFGSAVKLKnntttmA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHLLGNPEFAAPEVIQGIPVS--LGT-DIWSIGVLTYVMLSGVSP--FLDeskeetciNVCRVDF--------SFP 1203
Cdd:cd06626  158 PGEVNSLVGTPAYMAPEVITGNKGEghGRAaDIWSLGCVVLEMATGKRPwsELD--------NEWAIMYhvgmghkpPIP 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 68362740 1204 HEYfcGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06626  230 DSL--QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
992-1237 9.58e-23

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 99.33  E-value: 9.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDDG- 1066
Cdd:cd08228    9 KIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQdcvkEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGd 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 --RLLDYLMNHDELMEEKVAF-YIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLEDAVQISGHF-HIHH 1142
Cdd:cd08228   89 lsQMIKYFKKQKRLIPERTVWkYFVQLCSAVEHMHSRRVMHRDIKPANVFI---TATGVVKLGDLGLGRFFSSKTtAAHS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKE--ETCINVCRVDF-SFPHEYFcgvSNAARDFIN 1219
Cdd:cd08228  166 LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlfSLCQKIEQCDYpPLPTEHY---SEKLRELVS 242
                        250
                 ....*....|....*...
gi 68362740 1220 VILQEDFRRRPTAATCLQ 1237
Cdd:cd08228  243 MCIYPDPDQRPDIGYVHQ 260
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
987-1266 9.81e-23

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: 99.75  E-value: 9.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIdlEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISG-HFHIHHL 1143
Cdd:cd06642   86 GGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDtQIKRNTF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDFSFPHEYFCGV----SNAARDFIN 1219
Cdd:cd06642  162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSD-------LHPMRVLFLIPKNSPPTLegqhSKPFKEFVE 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1220 VILQEDFRRRPTAATCLQHPWLQphngSYSKiplDTSRLACFIERRK 1266
Cdd:cd06642  235 ACLNKDPRFRPTAKELLKHKFIT----RYTK---KTSFLTELIDRYK 274
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
987-1241 1.04e-22

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: 99.02  E-value: 1.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIdisRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHD--ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIH 1141
Cdd:cd08529   82 ENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD---KGDNVKIGDLGVAKILSDTTNFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 H-LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS-FPHEYfcgvSNAARDFIN 1219
Cdd:cd08529  159 QtIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASY----SQDLSQLID 234
                        250       260
                 ....*....|....*....|..
gi 68362740 1220 VILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd08529  235 SCLTKDYRQRPDTTELLRNPSL 256
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
993-1183 1.08e-22

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: 98.76  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKatRKDVAVK---FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKklkVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLmnHDELMEEKVAFYIR---DIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIH-HLLG 1145
Cdd:cd13999   79 DLL--HKKKIPLSWSLRLKialDIARGMNYLHSPPIIHRDLKSLNILLDEN---FTVKIADFGLSRIKNSTTEKMtGVVG 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 68362740 1146 NPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd13999  154 TPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF 191
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
989-1241 1.18e-22

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: 99.30  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNE-IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL-QHPQYITLHDTYESPTSYI------LIL 1060
Cdd:cd06608    9 ELVEvIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPGgddqlwLVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDG---RLLDYLMNHDELM-EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LED 1130
Cdd:cd06608   89 EYCGGGsvtDLVKGLRKKGKRLkEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE---AEVKLVDfgvsaqLDS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGHFhihhlLGNPEFAAPEVI---QGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVD---FSF 1202
Cdd:cd06608  166 TLGRRNTF-----IGTPYWMAPEVIacdQQPDASYDarCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPpptLKS 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 68362740 1203 PHEYfcgvSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06608  241 PEKW----SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
993-1190 1.19e-22

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: 98.98  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKA-TRKDVAVKFVSKKMKKKEQA--AHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNllGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL---RIPVP---RVKLIDLEDAVQISGHFHIHHL 1143
Cdd:cd14120   81 DYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgRKPSPndiRLKIADFGFARFLQDGMMAATL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE 1190
Cdd:cd14120  161 CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQE 207
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
987-1253 2.03e-22

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: 99.41  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINlQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH-LL 1144
Cdd:cd06655  101 GSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDFGFCAQITPEQSKRStMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDFSFPHEyfcgVSNAARDFINVI 1221
Cdd:cd06655  177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSPIFRDFLNRC 252
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1222 LQEDFRRRPTAATCLQHPWLQPHNGSYSKIPL 1253
Cdd:cd06655  253 LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPL 284
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
993-1229 2.69e-22

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: 99.31  E-value: 2.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAHEAA----LLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAiLKRNEVKHIMAernvLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL---EDAVQISGhfHIHHLL 1144
Cdd:cd05575   83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQ---GHVVLTDFglcKEGIEPSD--TTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQE 1224
Cdd:cd05575  158 GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRT----NVSPSARDLLEGLLQK 233

                 ....*
gi 68362740 1225 DFRRR 1229
Cdd:cd05575  234 DRTKR 238
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
993-1257 3.97e-22

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: 98.92  E-value: 3.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05601    9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVsffeEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLL--G 1145
Cdd:cd05601   89 LSLLSRYDDIFEESMArFYLAELVLAIHSLHSMGYVHRDIKPENILIDRT---GHIKLADFGSAAKLSSDKTVTSKMpvG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQGI------PVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPHEYfcGVSNAARDF 1217
Cdd:cd05601  166 TPDYIAPEVLTSMnggskgTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPEDP--KVSESAVDL 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 68362740 1218 INVILqEDFRRRPTAATCLQHPWlqphngsYSKIPLDTSR 1257
Cdd:cd05601  244 IKGLL-TDAKERLGYEGLCCHPF-------FSGIDWNNLR 275
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
987-1253 4.36e-22

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: 98.26  E-value: 4.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH-LL 1144
Cdd:cd06656  101 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRStMV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDFSFPHEyfcgVSNAARDFINVI 1221
Cdd:cd06656  177 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPER----LSAVFRDFLNRC 252
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1222 LQEDFRRRPTAATCLQHPWLQPHNGSYSKIPL 1253
Cdd:cd06656  253 LEMDVDRRGSAKELLQHPFLKLAKPLSSLTPL 284
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
990-1229 5.10e-22

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: 98.88  E-value: 5.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM--KKKEQ---AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVilNRKEQkhiMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDL---EDAVQISGhfHIH 1141
Cdd:cd05604   81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLD---SQGHIVLTDFglcKEGISNSD--TTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSF-PheyfcGVSNAARDFINV 1220
Cdd:cd05604  156 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLrP-----GISLTAWSILEE 230

                 ....*....
gi 68362740 1221 ILQEDFRRR 1229
Cdd:cd05604  231 LLEKDRQLR 239
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
993-1236 5.60e-22

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: 97.31  E-value: 5.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM----KKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLllkpHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHfHIHHLLGNPE 1148
Cdd:cd14187   95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEV-KIGDFGLATKVEYDGE-RKKTLCGTPN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 FAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQEDFRR 1228
Cdd:cd14187  173 YIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH----INPVAASLIQKMLQTDPTA 248

                 ....*...
gi 68362740 1229 RPTAATCL 1236
Cdd:cd14187  249 RPTINELL 256
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
993-1242 6.43e-22

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: 97.43  E-value: 6.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05605    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 L--DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd05605   88 KfhIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDH---GHVRISDLGLAVEIPEGETIRGRVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDE----SKEETCINVCRVdfsfPHEYFCGVSNAARDFINVIL 1222
Cdd:cd05605  165 VGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKED----QEEYSEKFSEEAKSICSQLL 240
                        250       260
                 ....*....|....*....|....*
gi 68362740 1223 QED--FR---RRPTAATCLQHPWLQ 1242
Cdd:cd05605  241 QKDpkTRlgcRGEGAEDVKSHPFFK 265
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
992-1242 1.18e-21

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: 96.74  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK-EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLlD 1070
Cdd:cd06611   12 ELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEElEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGAL-D 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH-LLGNP 1147
Cdd:cd06611   91 SIMLELErgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD---GDVKLADFGVSAKNKSTLQKRDtFIGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVI-----QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVD---FSFPHEYfcgvSNAARDFIN 1219
Cdd:cd06611  168 YWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKW----SSSFNDFLK 243
                        250       260
                 ....*....|....*....|...
gi 68362740 1220 VILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06611  244 SCLVKDPDDRPTAAELLKHPFVS 266
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
985-1239 1.65e-21

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: 95.89  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIdlEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLD---YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LEDAVQ 1133
Cdd:cd06610   81 LSGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGED---GSVKIADfgvsasLATGGD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISgHFHIHHLLGNPEFAAPEVI-QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF-SFPHEYFCGV- 1210
Cdd:cd06610  158 RT-RKVRKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPpSLETGADYKKy 236
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1211 SNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd06610  237 SKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
993-1229 1.88e-21

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: 97.00  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIiAKDEVAHtvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHLLGNP 1147
Cdd:cd05595   83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKD---GHIKITDFGLCKEgITDGATMKTFCGTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQEDFR 1227
Cdd:cd05595  160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRT----LSPEAKSLLAGLLKKDPK 235

                 ..
gi 68362740 1228 RR 1229
Cdd:cd05595  236 QR 237
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
993-1229 2.04e-21

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: 95.86  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05630    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 L--DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd05630   88 KfhIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDH---GHIRISDLGLAVHVPEGQTIKGRVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDF 1226
Cdd:cd05630  165 VGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDP 244

                 ...
gi 68362740 1227 RRR 1229
Cdd:cd05630  245 AER 247
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
987-1242 2.67e-21

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: 94.92  E-value: 2.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-------KKMKKKEQAAHEAALLQHL----QHPQYITLHDTYESPTS 1055
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISrnrvqqwSKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILILELMDDGR-LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipVPRVKLID------L 1128
Cdd:cd14101   82 FLLVLERPQHCQdLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLR--TGDIKLIDfgsgatL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQISghFHIHHLLGNPEFAAPEVIQGIPVSlgtdIWSIGVLTYVMLSGVSPFldESKEEtcinVCRVDFSFPHEyfc 1208
Cdd:cd14101  160 KDSMYTD--FDGTRVYSPPEWILYHQYHALPAT----VWSLGILLYDMVCGDIPF--ERDTD----ILKAKPSFNKR--- 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 68362740 1209 gVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14101  225 -VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
987-1239 2.71e-21

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: 95.06  E-value: 2.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd06613    2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKlEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH-LL 1144
Cdd:cd06613   82 GSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTED---GDVKLADFGVSAQLTATIAKRKsFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQ---GIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDFSFPHEYFCGV--------SNA 1213
Cdd:cd06613  159 GTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQPPMFD-------LHPMRALFLIPKSNFDPPklkdkekwSPD 231
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1214 ARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd06613  232 FHDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1031-1242 2.76e-21

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: 95.15  E-value: 2.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1031 EAALLQHL-QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKP 1109
Cdd:cd05583   48 ERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1110 ENLLIDLRipvPRVKLIDLedavQISGHF------HIHHLLGNPEFAAPEVIQGIPV--SLGTDIWSIGVLTYVMLSGVS 1181
Cdd:cd05583  128 ENILLDSE---GHVVLTDF----GLSKEFlpgendRAYSFCGTIEYMAPEVVRGGSDghDKAVDWWSLGVLTYELLTGAS 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1182 PFLDE----SKEETCINVCRVDFSFPHEYfcgvSNAARDFINVILQEDFRRR----PTAATCL-QHPWLQ 1242
Cdd:cd05583  201 PFTVDgernSQSEISKRILKSHPPIPKTF----SAEAKDFILKLLEKDPKKRlgagPRGAHEIkEHPFFK 266
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
993-1239 3.44e-21

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: 95.44  E-value: 3.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05631    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 L--DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd05631   88 KfhIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDR---GHIRISDLGLAVQIPEGETVRGRVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDF 1226
Cdd:cd05631  165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNP 244
                        250
                 ....*....|....*...
gi 68362740 1227 RRR-----PTAATCLQHP 1239
Cdd:cd05631  245 KERlgcrgNGAAGVKQHP 262
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
986-1239 4.85e-21

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 93.91  E-value: 4.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKfVSKKMKKKEQAAHE--AALLQHLQ---HPQYITLHDTYESPTSYILIL 1060
Cdd:cd14050    2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVK-RSRSRFRGEKDRKRklEEVERHEKlgeHPNCVRFIKAWEEKGILYIQT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDdGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHfHI 1140
Cdd:cd14050   81 ELCD-TSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKD---GVCKLGDFGLVVELDKE-DI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLL-GNPEFAAPEVIQGIPvSLGTDIWSIGVltyVMLSgVSPFLDESKEETCINVCRvDFSFPHEYFCGVSNAARDFIN 1219
Cdd:cd14050  156 HDAQeGDPRYMAPELLQGSF-TKAADIFSLGI---TILE-LACNLELPSGGDGWHQLR-QGYLPEEFTAGLSPELRSIIK 229
                        250       260
                 ....*....|....*....|
gi 68362740 1220 VILQEDFRRRPTAATCLQHP 1239
Cdd:cd14050  230 LMMDPDPERRPTAEDLLALP 249
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
986-1240 5.24e-21

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: 94.69  E-value: 5.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--------AAHEAALLQHLQHPQYITLHDTYE-SPTSY 1056
Cdd:cd13990    1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEkkqnyikhALREYEIHKSLDHPRIVKLYDVFEiDTDSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMdDGRLLDYLMNHDELMEEKVA-FYIRDIMEALQYLHNCR--VAHLDIKPENLLIDLRIPVPRVKLIDL----- 1128
Cdd:cd13990   81 CTVLEYC-DGNDLDFYLKQHKSIPEREArSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVSGEIKITDFglski 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 --EDAVQISGHFHIHHLLGNPEFAAPE--VIQGIP--VSLGTDIWSIGVLTYVMLSGVSPF------LDESKEETCINVC 1196
Cdd:cd13990  160 mdDESYNSDGMELTSQGAGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFghnqsqEAILEENTILKAT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 68362740 1197 RVDFSF-PHeyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd13990  240 EVEFPSkPV-----VSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
981-1241 7.22e-21

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 94.95  E-value: 7.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHlqhpqyITLHDTYESPTSYI--- 1057
Cdd:cd14136    6 EVYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKC------VREADPKDPGREHVvql 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 ---------------LILELMDDgRLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLIDlrIP 1119
Cdd:cd14136   80 lddfkhtgpngthvcMVFEVLGP-NLLKLIKRYNYrgIPLPLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLC--IS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1120 VPRVKLIDLEDAVQISGHF--HIHHLlgnpEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVspFL-------DESKEE 1190
Cdd:cd14136  157 KIEVKIADLGNACWTDKHFteDIQTR----QYRSPEVILGAGYGTPADIWSTACMAFELATGD--YLfdphsgeDYSRDE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1191 ---TCI---------NVCRVDfSFPHEYF--------------CGVSNAAR--------------DFINVILQEDFRRRP 1230
Cdd:cd14136  231 dhlALIiellgriprSIILSG-KYSREFFnrkgelrhisklkpWPLEDVLVekykwskeeakefaSFLLPMLEYDPEKRA 309
                        330
                 ....*....|.
gi 68362740 1231 TAATCLQHPWL 1241
Cdd:cd14136  310 TAAQCLQHPWL 320
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1026-1242 8.76e-21

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: 95.37  E-value: 8.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1026 EQAAHEAALLQHL-QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAH 1104
Cdd:cd05614   49 EHTRTERNVLEHVrQSPFLVTLHYAFQTDAKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1105 LDIKPENLLIDLRipvPRVKLIDLedavQISGHF------HIHHLLGNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVML 1177
Cdd:cd05614  129 RDIKLENILLDSE---GHVVLTDF----GLSKEFlteekeRTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELL 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1178 SGVSPFLDE----SKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQEDFRRR----PTAATCLQ-HPWLQ 1242
Cdd:cd05614  202 TGASPFTLEgeknTQSEVSRRILKCDPPFPSF----IGPVARDLLQKLLCKDPKKRlgagPQGAQEIKeHPFFK 271
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
987-1239 9.90e-21

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: 93.26  E-value: 9.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ---AAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEErqaALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNH-DELM-EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQISGHFHIH 1141
Cdd:cd08220   82 PGGTLFEYIQQRkGSLLsEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTV--VKIGDFGISKILSSKSKAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFcgvSNAARDFINVI 1221
Cdd:cd08220  160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRY---SEELRHLILSM 236
                        250
                 ....*....|....*...
gi 68362740 1222 LQEDFRRRPTAATCLQHP 1239
Cdd:cd08220  237 LHLDPNKRPTLSEIMAQP 254
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
986-1241 1.25e-20

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: 93.54  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVK-F--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd07833    2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkFkeSEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDgRLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISghfhih 1141
Cdd:cd07833   82 VER-TLLELLeASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVS---ESGVLKLCDFGFARALT------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 hllGNPE-----------FAAPEVIQGiPVSLG--TDIWSIGVLTYVMLSGVSPF------------------LDESKEE 1190
Cdd:cd07833  152 ---ARPAspltdyvatrwYRAPELLVG-DTNYGkpVDVWAIGCIMAELLDGEPLFpgdsdidqlyliqkclgpLPPSHQE 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1191 TCINVCRVD-FSFP---------HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07833  228 LFSSNPRFAgVAFPepsqpesleRRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
973-1229 1.56e-20

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: 94.76  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  973 DGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAH---EAALLQHLQHPQYITLHD 1048
Cdd:cd05593    3 DASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHtltESRVLKNTRHPFLTSLKY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1049 TYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL 1128
Cdd:cd05593   83 SFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD---GHIKITDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyf 1207
Cdd:cd05593  160 GLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT-- 237
                        250       260
                 ....*....|....*....|..
gi 68362740 1208 cgVSNAARDFINVILQEDFRRR 1229
Cdd:cd05593  238 --LSADAKSLLSGLLIKDPNKR 257
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
993-1240 1.71e-20

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: 92.78  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAAL------LQHLQHPQYITLHDTYESPTSYIL--ILELMD 1064
Cdd:cd06653   10 LGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALeceiqlLKNLRHDRIVQYYGCLRDPEEKKLsiFVEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQI-----SGHfH 1139
Cdd:cd06653   90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRD---SAGNVKLGDFGASKRIqticmSGT-G 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR--VDFSFPHeyfcGVSNAARDF 1217
Cdd:cd06653  166 IKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATqpTKPQLPD----GVSDACRDF 241
                        250       260
                 ....*....|....*....|...
gi 68362740 1218 INVILQEDfRRRPTAATCLQHPW 1240
Cdd:cd06653  242 LRQIFVEE-KRRPTAEFLLRHPF 263
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
993-1242 1.85e-20

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: 92.85  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM----KKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05609    8 ISNGAYGAVYLVRHRETRQRFAMKKINKQNlilrNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDL-------------------- 1128
Cdd:cd05609   88 ATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI---TSMGHIKLTDFglskiglmslttnlyeghie 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQisghFHIHHLLGNPEFAAPEVI----QGIPVslgtDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPH 1204
Cdd:cd05609  165 KDTRE----FLDKQVCGTPEYIAPEVIlrqgYGKPV----DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1205 EYFcGVSNAARDFINVILQEDFRRR---PTAATCLQHPWLQ 1242
Cdd:cd05609  237 GDD-ALPDDAQDLITRLLQQNPLERlgtGGAEEVKQHPFFQ 276
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
987-1253 2.03e-20

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: 93.25  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHH-LL 1144
Cdd:cd06654  102 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRStMV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDFSFPHEyfcgVSNAARDFINVI 1221
Cdd:cd06654  178 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIAtngTPELQNPEK----LSAIFRDFLNRC 253
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1222 LQEDFRRRPTAATCLQHPWLQPHNGSYSKIPL 1253
Cdd:cd06654  254 LEMDVEKRGSAKELLQHQFLKIAKPLSSLTPL 285
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
986-1229 2.10e-20

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: 93.02  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAaHEAALLQHL----QHPQYI-TLHDTYESPTSYILIL 1060
Cdd:cd05608    2 WFLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKG-YEGAMVEKRilakVHSRFIvSLAYAFQTKTDLCLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGRLLDYLMNHDE----LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQI-S 1135
Cdd:cd05608   81 TIMNGGDLRYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLD---DDGNVRISDLGLAVELkD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAAR 1215
Cdd:cd05608  158 GQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASK 237
                        250
                 ....*....|....
gi 68362740 1216 DFINVILQEDFRRR 1229
Cdd:cd05608  238 SICEALLAKDPEKR 251
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
992-1253 2.84e-20

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: 92.78  E-value: 2.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd06657   27 KIGEGSTGIVCIATVKSSGKLVAVKKMDlRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 yLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF-HIHHLLGNPEF 1149
Cdd:cd06657  107 -IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHD---GRVKLSDFGFCAQVSKEVpRRKSLVGTPYW 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1150 AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETcINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRR 1229
Cdd:cd06657  183 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA-MKMIRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR 261
                        250       260
                 ....*....|....*....|....
gi 68362740 1230 PTAATCLQHPWLQPHNGSYSKIPL 1253
Cdd:cd06657  262 ATAAELLKHPFLAKAGPPSCIVPL 285
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
993-1229 3.05e-20

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: 93.02  E-value: 3.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHiVSRSEVTHtlaERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL--RIPVPRVKLIDLedavQISGHFHIHHLLGN 1146
Cdd:cd05585   82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYtgHIALCDFGLCKL----NMKDDDKTNTFCGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQEDF 1226
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPD----GFDRDAKDLLIGLLNRDP 233

                 ...
gi 68362740 1227 RRR 1229
Cdd:cd05585  234 TKR 236
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
987-1240 4.60e-20

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: 91.95  E-value: 4.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH--EAALLQHLQ-HPQYITLHDT-YESPT-SYILILE 1061
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNlrEIQALRRLSpHPNILRLIEVlFDRKTgRLALVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDdgrlldylMNHDELM--------EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvprVKLIDLEDAVQ 1133
Cdd:cd07831   81 LMD--------MNLYELIkgrkrplpEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI----LKLADFGSCRG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGHfhihhllgnPEFA---------APEVI--QGIpVSLGTDIWSIGVLTYVMLSGVSPF--LDESKEETCI-NVC--- 1196
Cdd:cd07831  149 IYSK---------PPYTeyistrwyrAPECLltDGY-YGPKMDIWAVGCVFFEILSLFPLFpgTNELDQIAKIhDVLgtp 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1197 ------------RVDFSFPHEYFCG-------VSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07831  219 daevlkkfrksrHMNYNFPSKKGTGlrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
993-1242 4.79e-20

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: 92.73  E-value: 4.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05632   10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesmALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 L--DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd05632   90 KfhIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLD---DYGHIRISDLGLAVKIPEGESIRGRVGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDF 1226
Cdd:cd05632  167 VGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDP 246
                        250       260
                 ....*....|....*....|.
gi 68362740 1227 RRR-----PTAATCLQHPWLQ 1242
Cdd:cd05632  247 KQRlgcqeEGAGEVKRHPFFR 267
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
983-1237 5.63e-20

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: 91.59  E-value: 5.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTY-ESPTSYILi 1059
Cdd:cd13996    4 YLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIrlTEKSSASEKVLREVKALAKLNHPNIVRYYTAWvEEPPLYIQ- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYL--MNHDELMEEKVAF-YIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPR------VKLIdlED 1130
Cdd:cd13996   83 MELCEGGTLRDWIdrRNSSSKNDRKLALeLFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVKigdfglATSI--GN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGHFHIHHLLGNPE---------FAAPEVIQGIPVSLGTDIWSIGVLTYVMLsgvSPFLDESKEETCINVCRvDFS 1201
Cdd:cd13996  161 QKRELNNLNNNNNGNTSNnsvgigtplYASPEQLDGENYNEKADIYSLGIILFEML---HPFKTAMERSTILTDLR-NGI 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 68362740 1202 FPhEYFCGVSNAARDFINVILQEDFRRRPTAATCLQ 1237
Cdd:cd13996  237 LP-ESFKAKHPKEADLIQSLLSKNPEERPSAEQLLR 271
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
993-1279 6.71e-20

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: 92.28  E-value: 6.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAA-----LLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMtekrvLALANRHPFLTGLHACFQTEDRLYFVMEYVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL----EDavqISGHFHIHHL 1143
Cdd:cd05570   83 LMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAE---GHIKIADFgmckEG---IWGGNTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQ 1223
Cdd:cd05570  157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPR----WLSREAVSILKGLLT 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1224 EDFRRR----PTAATCLQ-HPWLQphngsyskiPLDTSRLacfiERRKhqndVRP--IPNVKS 1279
Cdd:cd05570  233 KDPARRlgcgPKGEADIKaHPFFR---------NIDWDKL----EKKE----VEPpfKPKVKS 278
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
1039-1279 9.63e-20

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: 91.68  E-value: 9.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1039 QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRi 1118
Cdd:cd05592   54 QHPFLTHLFCTFQTESHLFFVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDRE- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1119 pvPRVKLIDLEDAV-QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR 1197
Cdd:cd05592  133 --GHIKIADFGMCKeNIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICN 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1198 VDFSFPHEyfcgVSNAARDFINVILQEDFRRR-----PTAATCLQHPWLQphngsyskiPLDTSRLacfiERRkhqnDVR 1272
Cdd:cd05592  211 DTPHYPRW----LTKEAASCLSLLLERNPEKRlgvpeCPAGDIRDHPFFK---------TIDWDKL----ERR----EID 269

                 ....*....
gi 68362740 1273 P--IPNVKS 1279
Cdd:cd05592  270 PpfKPKVKS 278
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
993-1191 1.24e-19

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: 90.41  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVkkciHKATRKD---VAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd14066    1 IGSGGFGTV----YKGVLENgtvVAVKRLneMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDElmEEKVAFYIR-----DIMEALQYLHN---CRVAHLDIKPENLLIDlRIPVPRV------KLIDLEDAVQ 1133
Cdd:cd14066   77 LEDRLHCHKG--SPPLPWPQRlkiakGIARGLEYLHEecpPPIIHGDIKSSNILLD-EDFEPKLtdfglaRLIPPSESVS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1134 isghfHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEET 1191
Cdd:cd14066  154 -----KTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENAS 206
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
983-1245 1.30e-19

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: 91.97  E-value: 1.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTS---- 1055
Cdd:cd07851   13 VPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKrtyRELRLLKHMKHENVIGLLDVFTPASSledf 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 ---YiLILELMddGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLRIpvprvklIDL 1128
Cdd:cd07851   93 qdvY-LVTHLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVnedcELKI-------LDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQ----ISGHfhihhlLGNPEFAAPEVI-------QGIpvslgtDIWSIGVLTYVMLSGVSPF--LDESKEETCI-N 1194
Cdd:cd07851  163 GLARHtddeMTGY------VATRWYRAPEIMlnwmhynQTV------DIWSVGCIMAELLTGKTLFpgSDHIDQLKRImN 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1195 VC---------------------------RVDFsfpHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHN 1245
Cdd:cd07851  231 LVgtpdeellkkissesarnyiqslpqmpKKDF---KEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYH 305
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
977-1241 1.32e-19

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: 90.19  E-value: 1.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  977 ISWKENfdsaytelNEIGRGRFSIVKkCIHKATRKDVAVKFVSKKMKKKEQAA-------HEAALLQHLQHPQYITLHDT 1049
Cdd:cd06631    1 IQWKKG--------NVLGKGAYGTVY-CGLTSTGQLIAVKQVELDTSDKEKAEkeyeklqEEVDLLKTLKHVNIVGYLGT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1050 YESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLE 1129
Cdd:cd06631   72 CLEDNVVSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIML---MPNGVIKLIDFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1130 DA----VQISGHFH---IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSF 1202
Cdd:cd06631  149 CAkrlcINLSSGSQsqlLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPV 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1203 PH--EYFcgvSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06631  229 PRlpDKF---SPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
872-963 1.63e-19

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 84.47  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  872 PAAPNRPIAQERSCTSVILRWLPPSSTGNcTISGYTVEYREEGSQIWQQ-SVASTLDTYLVIEDLSPGCPYQFRVSASNP 950
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79
                         90
                 ....*....|...
gi 68362740  951 WGISLPSEPSEFV 963
Cdd:cd00063   80 GGESPPSESVTVT 92
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
987-1187 1.90e-19

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: 91.67  E-value: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd05596   28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSaffwEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI--SGHFHI 1140
Cdd:cd05596  108 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDAS---GHLKLADFGTCMKMdkDGLVRS 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1141 HHLLGNPEFAAPEVI--QGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDES 1187
Cdd:cd05596  184 DTAVGTPDYISPEVLksQGGDGVYGreCDWWSVGVFLYEMLVGDTPFYADS 234
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
987-1241 1.96e-19

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: 90.17  E-value: 1.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILEL- 1062
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIrleSEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 -MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFH 1139
Cdd:cd07861   82 sMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNK---GVIKLADfgLARAFGIPVRVY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLgNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV----------------DF-- 1200
Cdd:cd07861  159 THEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRIlgtptediwpgvtslpDYkn 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1201 SFPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07861  238 TFPKwkkgslrTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
993-1228 1.99e-19

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: 92.38  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQaahEAALLQHLQHP------QYIT-LHDTYESPTSYILILELMDD 1065
Cdd:cd05624   80 IGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRA---ETACFREERNVlvngdcQWITtLHYAFQDENYLYLVMDYYVG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMN-HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQIS--GHFHIHH 1142
Cdd:cd05624  157 GDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMN---GHIRLADFGSCLKMNddGTVQSSV 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGT-----DIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVD--FSFPhEYFCGVSNAAR 1215
Cdd:cd05624  234 AVGTPDYISPEILQAMEDGMGKygpecDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerFQFP-SHVTDVSEEAK 312
                        250
                 ....*....|...
gi 68362740 1216 DFINVILQEDFRR 1228
Cdd:cd05624  313 DLIQRLICSRERR 325
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
981-1241 2.01e-19

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: 91.09  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQH--PQY----ITLHDTYESPT 1054
Cdd:cd14134    8 DLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEkdPNGkshcVQLRDWFDYRG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 SYILILELMddGR-LLDYLMNHDelME----EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--------------- 1114
Cdd:cd14134   88 HMCIVFELL--GPsLYDFLKKNN--YGpfplEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynpkkkr 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1115 DLRIPV-PRVKLIDLEDAVqisghF-HIHH--LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF------- 1183
Cdd:cd14134  164 QIRVPKsTDIKLIDFGSAT-----FdDEYHssIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqthdnle 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1184 ---------------------------------LDESKEETCIN----VCRVDFSFP------HEYFCgvsnaarDFINV 1220
Cdd:cd14134  239 hlammerilgplpkrmirrakkgakyfyfyhgrLDWPEGSSSGRsikrVCKPLKRLMllvdpeHRLLF-------DLIRK 311
                        330       340
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14134  312 MLEYDPSKRITAKEALKHPFF 332
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
985-1245 2.23e-19

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: 91.09  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYI-LIL 1060
Cdd:cd07856   10 TRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRtyrELKLLKHLRHENIISLSDIFISPLEDIyFVT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMddGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLRIpvPRVKLIDLEDAvQISG 1136
Cdd:cd07856   90 ELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVnencDLKI--CDFGLARIQDP-QMTG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHllgnpeFAAPEVI---QGIPVSLgtDIWSIGVLTYVMLSG---------------VSPFLDESKEETCINVC-- 1196
Cdd:cd07856  165 YVSTRY------YRAPEIMltwQKYDVEV--DIWSAGCIFAEMLEGkplfpgkdhvnqfsiITELLGTPPDDVINTICse 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68362740 1197 ---RVDFSFPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHN 1245
Cdd:cd07856  237 ntlRFVQSLPKrervpfsEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYH 295
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
987-1242 2.46e-19

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: 90.02  E-value: 2.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK---------------------------EQAAHEAALLQHLQ 1039
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqprgpiERVYQEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1040 HPQYITLHDTYESPTS--YILILELMDDGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlr 1117
Cdd:cd14199   84 HPNVVKLVEVLDDPSEdhLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1118 iPVPRVKLIDLEDAVQISGH-FHIHHLLGNPEFAAPEVI---QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCI 1193
Cdd:cd14199  161 -EDGHIKIADFGVSNEFEGSdALLTNTVGTPAFMAPETLsetRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 68362740 1194 NVCRVDFSFPHEYfcGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd14199  240 KIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
987-1266 3.27e-19

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: 89.34  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd06640    6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIdlEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISG-HFHIHHL 1143
Cdd:cd06640   86 GGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDtQIKRNTF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDF---SFPHEYFCG-VSNAARDFIN 1219
Cdd:cd06640  162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSD-------MHPMRVLFlipKNNPPTLVGdFSKPFKEFID 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1220 VILQEDFRRRPTAATCLQHPWLQPHNGSyskipldTSRLACFIERRK 1266
Cdd:cd06640  235 ACLNKDPSFRPTAKELLKHKFIVKNAKK-------TSYLTELIDRFK 274
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
993-1241 3.62e-19

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: 88.98  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA-----------HEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADsrqktvvdalkSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLripvprvklidlEDAVQIS--GHF- 1138
Cdd:cd06629   89 YVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDL------------EGICKISdfGISk 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHHLLGNPE---------FAAPEVI--QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYF 1207
Cdd:cd06629  157 KSDDIYGNNGatsmqgsvfWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVPED 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 68362740 1208 CGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06629  237 VNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
990-1232 3.68e-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: 88.98  E-value: 3.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRkdVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITL--HDTYESPTSYILILELMDD 1065
Cdd:cd13979    8 QEPLGSGGFGSVYKATYKGET--VAVKIVrrRRKNRASRQSFWAELNAARLRHENIVRVlaAETGTDFASLGLIIMEYCG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMN--HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLR-IPvprvKLIDLEDAVQISG----HF 1138
Cdd:cd13979   86 NGTLQQLIYegSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQgVC----KLCDFGCSVKLGEgnevGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDEsKEETCINVC----RVDFSFPHEYFCGvsNAA 1214
Cdd:cd13979  162 PRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGL-RQHVLYAVVakdlRPDLSGLEDSEFG--QRL 238
                        250
                 ....*....|....*...
gi 68362740 1215 RDFINVILQEDFRRRPTA 1232
Cdd:cd13979  239 RSLISRCWSAQPAERPNA 256
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
986-1238 4.28e-19

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: 88.45  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK----EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd14189    2 SYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKphqrEKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQI-SGHFHI 1140
Cdd:cd14189   82 LCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENM---ELKVGDFGLAARLePPEQRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPheyfCGVSNAARDFINV 1220
Cdd:cd14189  159 KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLP----ASLSLPARHLLAG 234
                        250
                 ....*....|....*...
gi 68362740 1221 ILQEDFRRRPTAATCLQH 1238
Cdd:cd14189  235 ILKRNPGDRLTLDQILEH 252
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
983-1241 5.65e-19

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: 88.23  E-value: 5.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNE---IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEA-ALLQHLQHP---QYITlhdtYESPTS 1055
Cdd:cd06624    3 YEYEYDESGErvvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEiALHSRLSHKnivQYLG----SVSEDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILI-LELMDDGRLLDY-------LMNHdelmEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLID 1127
Cdd:cd06624   79 FFKIfMEQVPGGSLSALlrskwgpLKDN----ENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGV--VKISD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1128 LEDAVQISG-HFHIHHLLGNPEFAAPEVIQGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCInvCRVDFSFPH 1204
Cdd:cd06624  153 FGTSKRLAGiNPCTETFTGTLQYMAPEVIDKGQRGYGppADIWSLGCTIIEMATGKPPFIELGEPQAAM--FKVGMFKIH 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 68362740 1205 -EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06624  231 pEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
993-1182 6.38e-19

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: 88.15  E-value: 6.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYI--TLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIikTYDVAFETEDYYVFAQEYAPYGDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI---DLRipvpRVKLIDLeDAVQISGHFhIHHLLGNP 1147
Cdd:cd13987   81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdkDCR----RVKLCDF-GLTRRVGST-VKRVSGTI 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIP-----VSLGTDIWSIGVLTYVMLSGVSP 1182
Cdd:cd13987  155 PYTAPEVCEAKKnegfvVDPSIDVWAFGVLLFCCLTGNFP 194
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
987-1285 7.23e-19

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: 90.44  E-value: 7.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd05621   54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSaffwEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQI--SGHFHI 1140
Cdd:cd05621  134 MPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLD---KYGHLKLADFGTCMKMdeTGMVHC 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVI--QGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPHEyfCGVSNAA 1214
Cdd:cd05621  210 DTAVGTPDYISPEVLksQGGDGYYGreCDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDD--VEISKHA 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1215 RDFINVILQEDFRR--RPTAATCLQHPWLQPHNGSYSKI-------------PLDTSRlacFIERRKHQNDVRPIPNVKS 1279
Cdd:cd05621  288 KNLICAFLTDREVRlgRNGVEEIKQHPFFRNDQWNWDNIretaapvvpelssDIDTSN---FDDIEDDKGDVETFPIPKA 364

                 ....*.
gi 68362740 1280 YIVNRV 1285
Cdd:cd05621  365 FVGNQL 370
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
988-1241 8.44e-19

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: 88.25  E-value: 8.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  988 TELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM--KKKEQAAHEAALLQHLQHPQYITLHDTY--ESPTSYILILELM 1063
Cdd:cd06621    4 VELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPnpDVQKQILRELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDG-------RLLDYLMNHDELMEEKVAFyirDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL----EDAV 1132
Cdd:cd06621   84 EGGsldsiykKVKKKGGRIGEKVLGKIAE---SVLKGLSYLHSRKIIHRDIKPSNILLTRK---GQVKLCDFgvsgELVN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFhihhlLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESK------EETCINVCRVDFSFPHEY 1206
Cdd:cd06621  158 SLAGTF-----TGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEpplgpiELLSYIVNMPNPELKDEP 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 68362740 1207 FCGV--SNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06621  233 ENGIkwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWI 269
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
987-1241 8.87e-19

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: 87.71  E-value: 8.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK---FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKeidLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYL-MNHDELMEE-KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQISGHFHIH 1141
Cdd:cd08225   82 DGGDLMKRInRQRGVLFSEdQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMV--AKLGDFGIARQLNDSMELA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HL-LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFsfpHEYFCGVSNAARDFINV 1220
Cdd:cd08225  160 YTcVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYF---APISPNFSRDLRSLISQ 236
                        250       260
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd08225  237 LFKVSPRDRPSITSILKRPFL 257
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
987-1241 9.74e-19

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: 88.08  E-value: 9.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK---------------------------EQAAHEAALLQHLQ 1039
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKqygfprrppprgskaaqgeqakplaplERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1040 HPQYITLHDTYESPT--SYILILELMDDGRLLDYLMNHdELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlr 1117
Cdd:cd14200   82 HVNIVKLIEVLDDPAedNLYMVFDLLRKGPVMEVPSDK-PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1118 iPVPRVKLIDLEDAVQISGH-FHIHHLLGNPEFAAPEVIQGIPVSL---GTDIWSIGVLTYVMLSGVSPFLDESKEETCI 1193
Cdd:cd14200  159 -DDGHVKIADFGVSNQFEGNdALLSSTAGTPAFMAPETLSDSGQSFsgkALDVWAMGVTLYCFVYGKCPFIDEFILALHN 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1194 NVCRVDFSFPHEyfCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14200  238 KIKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
974-1241 1.04e-18

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: 88.14  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  974 GATISWKENFDSAYT-ELNE-IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQ-HPQYITLHDTY 1050
Cdd:cd06638    5 GKTIIFDSFPDPSDTwEIIEtIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSdHPNVVKFYGMY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1051 -----ESPTSYILILELMDDGRLLD----YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvP 1121
Cdd:cd06638   85 ykkdvKNGDQLWLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE---G 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1122 RVKLIDLEDAVQISGHFHIHHL-LGNPEFAAPEVI---QGIPVSLGT--DIWSIGVLTYVMLSGVSPFLDeskeetcINV 1195
Cdd:cd06638  162 GVKLVDFGVSAQLTSTRLRRNTsVGTPFWMAPEVIaceQQLDSTYDArcDVWSLGITAIELGDGDPPLAD-------LHP 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1196 CRVDFSFPH---------EYFcgvSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06638  235 MRALFKIPRnppptlhqpELW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
993-1245 1.52e-18

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: 88.18  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEViIAKDEVAHtltENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL----EDavqISGHFHIHHLL 1144
Cdd:cd05571   83 FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKD---GHIKITDFglckEE---ISYGATTKTFC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQE 1224
Cdd:cd05571  157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPS----TLSPEAKSLLAGLLKK 232
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1225 DFRRR-----PTAATCLQHPWLQPHN 1245
Cdd:cd05571  233 DPKKRlgggpRDAKEIMEHPFFASIN 258
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
987-1236 1.67e-18

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: 86.57  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS--KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRlpKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELM--EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQIS--GHFHI 1140
Cdd:cd08219   82 GGDLMQKIKLQRGKLfpEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQN---GKVKLGDFGSARLLTspGAYAC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLlGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS-FPHEYfcgvSNAARDFIN 1219
Cdd:cd08219  159 TYV-GTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHY----SYELRSLIK 233
                        250
                 ....*....|....*..
gi 68362740 1220 VILQEDFRRRPTAATCL 1236
Cdd:cd08219  234 QMFKRNPRSRPSATTIL 250
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
987-1241 2.00e-18

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: 86.45  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQkflpRELSILRRVNHPNIVQMFECIEVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLidLRIPVPRVKLIDLEDAVQISGHFHIHH 1142
Cdd:cd14164   82 AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENIL--LSADDRKIKIADFGFARFVEDYPELST 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LL-GNPEFAAPEVIQGIPVSLGT-DIWSIGVLTYVMLSGVSPFldeskEETCINVCRVDfSFPHEYFCGVS--NAARDFI 1218
Cdd:cd14164  160 TFcGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGTMPF-----DETNVRRLRLQ-QRGVLYPSGVAleEPCRALI 233
                        250       260
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14164  234 RTLLQFNPSTRPSIQQVAGNSWL 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
988-1190 2.08e-18

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 86.43  E-value: 2.08e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     988 TELNEIGRGRFSIVKKCI----HKATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:smart00219    2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQIEEflREARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    1062 LMDDGRLLDYLMNHDE--LMEEKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFH 1139
Cdd:smart00219   82 YMEGGDLLSYLRKNRPklSLSDLLSF-ALQIARGMEYLESKNFIHRDLAARNCLVGEN---LVVKISDFGLSRDLYDDDY 157
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740    1140 IHHLLGN-PEF-AAPEVIQ-GIpVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEE 1190
Cdd:smart00219  158 YRKRGGKlPIRwMAPESLKeGK-FTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE 211
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1044-1241 2.16e-18

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: 86.16  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1044 ITLHDTYESPTSYILILE---LMDDgrLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipV 1120
Cdd:cd14102   67 IKLLDWYERPDGFLIVMErpePVKD--LFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR--T 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1121 PRVKLID------LEDAVQISghFHIHHLLGNPEFAAPEVIQGIPVSlgtdIWSIGVLTYVMLSGVSPFldESKEEtcin 1194
Cdd:cd14102  143 GELKLIDfgsgalLKDTVYTD--FDGTRVYSPPEWIRYHRYHGRSAT----VWSLGVLLYDMVCGDIPF--EQDEE---- 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1195 VCRVDFSFPHEyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14102  211 ILRGRLYFRRR----VSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
984-1229 2.89e-18

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: 86.88  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKK----MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILI 1059
Cdd:cd05607    1 DKYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKrlkkKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGH 1137
Cdd:cd05607   81 MSLMNGGDLKYHIYNVGErgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDN---GNCRLSDLGLAVEVKEG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDE----SKEETCINVCRVDFSFPHEYFcgvSNA 1213
Cdd:cd05607  158 KPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFEHQNF---TEE 234
                        250
                 ....*....|....*.
gi 68362740 1214 ARDFINVILQEDFRRR 1229
Cdd:cd05607  235 AKDICRLFLAKKPENR 250
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
988-1190 2.94e-18

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: 86.06  E-value: 2.94e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     988 TELNEIGRGRFSIVKKCIHKA----TRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:smart00221    2 TLGKKLGEGAFGEVYKGTLKGkgdgKEVEVAVKTLKEDASEQQIEEflREARIMRKLDHPNIVKLLGVCTEEEPLMIVME 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    1062 LMDDGRLLDYLMNHDEL---MEEKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF 1138
Cdd:smart00221   82 YMPGGDLLDYLRKNRPKelsLSDLLSF-ALQIARGMEYLESKNFIHRDLAARNCLVGEN---LVVKISDFGLSRDLYDDD 157
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740    1139 HIHHLLGN-PEF-AAPEVIQ-GIpVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEE 1190
Cdd:smart00221  158 YYKVKGGKlPIRwMAPESLKeGK-FTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAE 212
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
1031-1204 3.62e-18

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: 87.07  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1031 EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPE 1110
Cdd:cd05582   47 ERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPE 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1111 NLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKE 1189
Cdd:cd05582  127 NILLDED---GHIKLTDFGLSKEsIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRK 203
                        170
                 ....*....|....*
gi 68362740 1190 ETCINVCRVDFSFPH 1204
Cdd:cd05582  204 ETMTMILKAKLGMPQ 218
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
990-1242 4.15e-18

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: 86.20  E-value: 4.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL-QHPQYITLHDTYESPTSYI-----LILELM 1063
Cdd:cd06639   27 IETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQYVggqlwLVLELC 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDY----LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI-SGHF 1138
Cdd:cd06639  107 NGGSVTELvkglLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVDFGVSAQLtSARL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHHLLGNPEFAAPEVI---QGIPVSLGT--DIWSIGVLTYVMLSGVSPFLDESKEETCINVCR---VDFSFPHEYFCGV 1210
Cdd:cd06639  184 RRNTSVGTPFWMAPEVIaceQQYDYSYDArcDVWSLGITAIELADGDPPLFDMHPVKALFKIPRnppPTLLNPEKWCRGF 263
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1211 SNaardFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06639  264 SH----FISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
987-1241 4.57e-18

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: 85.89  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdlEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISG-HFHIHHL 1143
Cdd:cd06641   86 GGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEH---GEVKLADFGVAGQLTDtQIKRN*F 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDFSFPHE----YFCGVSNAARDFIN 1219
Cdd:cd06641  162 VGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSE-------LHPMKVLFLIPKNnpptLEGNYSKPLKEFVE 234
                        250       260
                 ....*....|....*....|..
gi 68362740 1220 VILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06641  235 ACLNKEPSFRPTAKELLKHKFI 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
993-1238 4.89e-18

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: 85.48  E-value: 4.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH------EAALLQHLQHPQ----YITLHDTYESPTSyiLILEL 1062
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEvnalecEIQLLKNLLHERivqyYGCLRDPQERTLS--IFMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLE-----DAVQISGH 1137
Cdd:cd06652   88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRD---SVGNVKLGDFGaskrlQTICLSGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 fHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS---FPHeyfcgVSNAA 1214
Cdd:cd06652  165 -GMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNpqlPAH-----VSDHC 238
                        250       260
                 ....*....|....*....|....
gi 68362740 1215 RDFINVILQEDfRRRPTAATCLQH 1238
Cdd:cd06652  239 RDFLKRIFVEA-KLRPSADELLRH 261
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
987-1241 5.30e-18

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: 85.79  E-value: 5.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKkkEQAA-----HEAALLQHLQ---HPQYITLHD-----TYESP 1053
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLS--EEGIplstiREIALLKQLEsfeHPNVVRLLDvchgpRTDRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMD-DgrLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLED 1130
Cdd:cd07838   79 LKLTLVFEHVDqD--LATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSD---GQVKLADFGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF--------LDE--------SKEETCIN 1194
Cdd:cd07838  154 ARIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFrgsseadqLGKifdviglpSEEEWPRN 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1195 VCRVDFSFPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07838  234 SALPRSSFPSytprpfkSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1044-1241 5.39e-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: 85.02  E-value: 5.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1044 ITLHDTYESPTSYILILELMDDGR-LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipVPR 1122
Cdd:cd14100   68 IRLLDWFERPDSFVLVLERPEPVQdLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLN--TGE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1123 VKLID------LEDAVQISghFHIHHLLGNPEFAAPEVIQGIPVSlgtdIWSIGVLTYVMLSGVSPFldESKEEtcinVC 1196
Cdd:cd14100  146 LKLIDfgsgalLKDTVYTD--FDGTRVYSPPEWIRFHRYHGRSAA----VWSLGILLYDMVCGDIPF--EHDEE----II 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 68362740 1197 RVDFSFPHEyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14100  214 RGQVFFRQR----VSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
986-1241 5.78e-18

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: 85.90  E-value: 5.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMkkkEQAA-----HEAALLQHLQHPQYITLHDTYESPTSYILIL 1060
Cdd:cd07844    1 TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEH---EEGApftaiREASLLKDLKHANIVTLHDIIHTKKTLTLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGrLLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGH 1137
Cdd:cd07844   78 EYLDTD-LKQYMDDCGGGLSmHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISER---GELKLADfgLARAKSVPSK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHH-----------LLGNPEFAAPeviqgipvslgTDIWSIGVLTYVMLSGVSPF----------------LDESKEE 1190
Cdd:cd07844  154 TYSNEvvtlwyrppdvLLGSTEYSTS-----------LDMWGVGCIFYEMATGRPLFpgstdvedqlhkifrvLGTPTEE 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1191 T----CINVCRVDFSFPH---EYFC------GVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07844  223 TwpgvSSNPEFKPYSFPFyppRPLInhaprlDRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
981-1218 6.08e-18

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 87.40  E-value: 6.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSayteLNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAH---EAALLQHLQHPQYITLHDTYESPTSY 1056
Cdd:cd05628    1 EDFES----LKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMlEKEQVGHiraERDILVEADSLWVVKMFYSFQDKLNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LED 1130
Cdd:cd05628   77 YLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDfglctgLKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGHFHIHHLL------------------------------GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGV 1180
Cdd:cd05628  154 AHRTEFYRNLNHSLpsdftfqnmnskrkaetwkrnrrqlafstvGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGY 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 68362740 1181 SPFLDESKEETCINVC--RVDFSFPHEyfCGVSNAARDFI 1218
Cdd:cd05628  234 PPFCSETPQETYKKVMnwKETLIFPPE--VPISEKAKDLI 271
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
990-1240 8.09e-18

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 86.25  E-value: 8.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQaahEAALLQH----LQH--PQYIT-LHDTYESPTSYILILEL 1062
Cdd:cd05597    6 LKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRA---ETACFREerdvLVNgdRRWITkLHYAFQDENYLYLVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI--SGHFH 1139
Cdd:cd05597   83 YCGGDLLTLLSKFeDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRN---GHIRLADFGSCLKLreDGTVQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPEFAAPEVIQGIPVSLGT-----DIWSIGVLTYVMLSGVSPFLDESKEETcinVCRV-----DFSFPhEYFCG 1209
Cdd:cd05597  160 SSVAVGTPDYISPEILQAMEDGKGRygpecDWWSLGVCMYEMLYGETPFYAESLVET---YGKImnhkeHFSFP-DDEDD 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 68362740 1210 VSNAARDFINVILQEDFRR--RPTAATCLQHPW 1240
Cdd:cd05597  236 VSEEAKDLIRRLICSRERRlgQNGIDDFKKHPF 268
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
987-1244 8.20e-18

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: 86.04  E-value: 8.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHD--TYESPTSY---IL 1058
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRilrEIKILRHLKHENIIGLLDilRPPSPEEFndvYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1059 ILELMD-DgrlLDYLM-NHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLripvprvKLIDLEDAV 1132
Cdd:cd07834   82 VTELMEtD---LHKVIkSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVnsncDL-------KICDFGLAR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLlgnPEFA------APEVI-------QGIpvslgtDIWSIGVL--------------TYV-MLS------ 1178
Cdd:cd07834  152 GVDPDEDKGFL---TEYVvtrwyrAPELLlsskkytKAI------DIWSVGCIfaelltrkplfpgrDYIdQLNlivevl 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1179 GVSP--FLDESKEETCIN-------VCRVDFSfphEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd07834  223 GTPSeeDLKFISSEKARNylkslpkKPKKPLS---EVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
992-1230 8.51e-18

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: 85.47  E-value: 8.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDDG- 1066
Cdd:cd08229   31 KIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARAdcikEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGd 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 --RLLDYLMNHDELMEEKVAF-YIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLEDAVQISGHF-HIHH 1142
Cdd:cd08229  111 lsRMIKHFKKQKRLIPEKTVWkYFVQLCSALEHMHSRRVMHRDIKPANVFI---TATGVVKLGDLGLGRFFSSKTtAAHS 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKE--ETCINVCRVDF-SFPHEYFcgvSNAARDFIN 1219
Cdd:cd08229  188 LVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNlySLCKKIEQCDYpPLPSDHY---SEELRQLVN 264
                        250
                 ....*....|.
gi 68362740 1220 VILQEDFRRRP 1230
Cdd:cd08229  265 MCINPDPEKRP 275
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
987-1218 9.79e-18

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: 86.65  E-value: 9.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMK-KKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd05627    4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMlEKEQVAHiraERDILVEADGAWVVKMFYSFQDKRNLYLIMEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LEDAVQISG 1136
Cdd:cd05627   84 LPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDfglctgLKKAHRTEF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHH------------------------------LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDE 1186
Cdd:cd05627  161 YRNLTHnppsdfsfqnmnskrkaetwkknrrqlaysTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 68362740 1187 SKEETCINVC--RVDFSFPHEyfCGVSNAARDFI 1218
Cdd:cd05627  241 TPQETYRKVMnwKETLVFPPE--VPISEKAKDLI 272
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
1039-1245 1.19e-17

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: 85.38  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1039 QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRi 1118
Cdd:cd05620   54 ENPFLTHLYCTFQTKEHLFFVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRD- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1119 pvPRVKLIDLEDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVcR 1197
Cdd:cd05620  133 --GHIKIADFGMCKEnVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI-R 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 68362740 1198 VDfsFPHeYFCGVSNAARDFINVILQED-FRRRPTAATCLQHPWLQPHN 1245
Cdd:cd05620  210 VD--TPH-YPRWITKESKDILEKLFERDpTRRLGVVGNIRGHPFFKTIN 255
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
989-1239 1.30e-17

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: 83.97  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNEIGRGRFSIVKKCIHKATRKDVAVK--------FVSKKMKKKEQAAHEAALlqhlQHPQYITLHDTYESPTSYILIL 1060
Cdd:cd13997    4 ELEQIGSGSFSEVFKVRSKVDGCLYAVKkskkpfrgPKERARALREVEAHAALG----QHPNIVRYYSSWEEGGHLYIQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGRL---LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGH 1137
Cdd:cd13997   80 ELCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKG---TCKIGDFGLATRLETS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHllGNPEFAAPEVIQGIPVSL-GTDIWSIGVLTYVMLSGvSPFLDesKEETCINVCRVDFSFPHEyfCGVSNAARD 1216
Cdd:cd13997  157 GDVEE--GDSRYLAPELLNENYTHLpKADIFSLGVTVYEAATG-EPLPR--NGQQWQQLRQGKLPLPPG--LVLSQELTR 229
                        250       260
                 ....*....|....*....|...
gi 68362740 1217 FINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd13997  230 LLKVMLDPDPTRRPTADQLLAHD 252
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
990-1229 2.37e-17

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: 85.47  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05594   30 LKLLGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVAHtltENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR-VAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHL 1143
Cdd:cd05594  110 GELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKD---GHIKITDFGLCKEgIKDGATMKTF 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFINVILQ 1223
Cdd:cd05594  187 CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRT----LSPEAKSLLSGLLK 262

                 ....*.
gi 68362740 1224 EDFRRR 1229
Cdd:cd05594  263 KDPKQR 268
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
985-1218 2.72e-17

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: 84.68  E-value: 2.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRF---SIVKKcihKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYI 1057
Cdd:cd05598    1 SMFEKIKTIGVGAFgevSLVRK---KDTNALYAMKTLRKKDvLKRNQVAHvkaERDILAEADNEWVVKLYYSFQDKENLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMNHdELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL-------- 1128
Cdd:cd05598   78 FVMDYIPGGDLMSLLIKK-GIFEEDLArFYIAELVCAIESVHKMGFIHRDIKPDNILIDRD---GHIKLTDFglctgfrw 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 -EDavqiSGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPHE 1205
Cdd:cd05598  154 tHD----SKYYLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHE 229
                        250
                 ....*....|...
gi 68362740 1206 yfCGVSNAARDFI 1218
Cdd:cd05598  230 --ANLSPEAKDLI 240
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
980-1230 3.24e-17

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 85.45  E-value: 3.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  980 KENFDSayteLNEIGRGRFSIVKKCIHKATRKDVAVKFVSK--KMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTS 1055
Cdd:cd05623   71 KEDFEI----LKVIGRGAFGEVAVVKLKNADKVFAMKILNKweMLKRAETACfrEERDVLVNGDSQWITTLHYAFQDDNN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILILELMDDGRLLDYLMN-HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI 1134
Cdd:cd05623  147 LYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMN---GHIRLADFGSCLKL 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1135 --SGHFHIHHLLGNPEFAAPEVIQGIPVSLGT-----DIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPHE 1205
Cdd:cd05623  224 meDGTVQSSVAVGTPDYISPEILQAMEDGKGKygpecDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKERFQFPTQ 303
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 68362740 1206 yFCGVSNAARDFINVIL-----------QEDFRRRP 1230
Cdd:cd05623  304 -VTDVSENAKDLIRRLIcsrehrlgqngIEDFKNHP 338
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
987-1240 4.05e-17

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: 83.39  E-value: 4.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ------AAHEAALLQHLQHPQYITLHDTYESPTSYILIL 1060
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdginftALREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMD--------DGRLLdylmnhdeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAV 1132
Cdd:cd07841   82 EFMEtdlekvikDKSIV--------LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA---SDGVLKLADFGLAR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QI-SGHFHIHHLLGNPEFAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGVsPFLD-ES---------------KEETCIN 1194
Cdd:cd07841  151 SFgSPNRKMTHQVVTRWYRAPELLFGARHyGVGVDMWSVGCIFAELLLRV-PFLPgDSdidqlgkifealgtpTEENWPG 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1195 VCR----VDFS-FP----HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07841  230 VTSlpdyVEFKpFPptplKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
987-1285 5.27e-17

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: 85.06  E-value: 5.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd05622   75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSaffwEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQIS--GHFHI 1140
Cdd:cd05622  155 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD---KSGHLKLADFGTCMKMNkeGMVRC 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVI--QGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVC--RVDFSFPHEyfCGVSNAA 1214
Cdd:cd05622  231 DTAVGTPDYISPEVLksQGGDGYYGreCDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPDD--NDISKEA 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1215 RDFINVILQEDFRR--RPTAATCLQHPWLQPHNGSYSKI-------------PLDTSRLACfIERRKHQNDVRPIPnvKS 1279
Cdd:cd05622  309 KNLICAFLTDREVRlgRNGVEEIKRHLFFKNDQWAWETLrdtvapvvpdlssDIDTSNFDD-LEEDKGEEETFPIP--KA 385

                 ....*.
gi 68362740 1280 YIVNRV 1285
Cdd:cd05622  386 FVGNQL 391
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
987-1252 8.26e-17

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: 82.74  E-value: 8.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd07873    4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGrLLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFHIH 1141
Cdd:cd07873   84 KD-LKQYLDDCGNSINmHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADfgLARAKSIPTKTYSN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLgNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV-------------------DFS 1201
Cdd:cd07873  160 EVV-TLWYRPPDILLGsTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRIlgtpteetwpgilsneefkSYN 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1202 FPHEYF-CGVSNAAR------DFINVILQEDFRRRPTAATCLQHPWLQPHNGSYSKIP 1252
Cdd:cd07873  239 YPKYRAdALHNHAPRldsdgaDLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIHKLP 296
PH1_Kalirin_Trio_like cd13240
Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; ...
413-529 1.08e-16

Triple functional domain pleckstrin homology pleckstrin homology (PH) domain, repeat 1; RhoGEFs, Kalirin and Trio, the mammalian homologs of Drosophila Trio and Caenorhabditis elegans UNC-73 regulate a novel step in secretory granule maturation. Their signaling modulates the extent to which regulated cargo enter and remain in the regulated secretory pathway. This allows for fine tuning of peptides released by a single secretory cell type with impaired signaling leading to pathological states. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Kalirin and Trio are encoded by separate genes in mammals and by a single one in invertebrates. Kalirin and Trio share the same complex multidomain structure and display several splice variants. The longest Kalirin and Trio proteins have a Sec14 domain, a stretch of spectrin repeats, a RhoGEF(DH)/PH cassette (also called GEF1), an SH3 domain, a second RhoGEF(DH)/PH cassette (also called GEF2), a second SH3 domain, Ig/FNIII domains, and a kinase domain. The first RhoGEF(DH)/PH cassette catalyzes exchange on Rac1 and RhoG while the second RhoGEF(DH)/PH cassette is specific for RhoA. Kalirin and Trio are closely related to p63RhoGEF and have PH domains of similar function. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains.


Pssm-ID: 270060  Cd Length: 123  Bit Score: 77.42  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  413 LQGFEGTLTAQGKLLQQDTFYVIELDAgMQSRTKERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYLVLEENVDND 492
Cdd:cd13240    2 LEGCDEDLDSLGEVILQDSFQVWDPKQ-LIRKGRERHVFLFELCLVFSKEVKDSNGKSKYIYKSRLMTSEIGVTEHIEGD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 68362740  493 PCKFALMNRE--TSE-RVVLQAANADIQQAWVQDINQVLE 529
Cdd:cd13240   81 PCKFALWTGRvpTSDnKIVLKASSLEVKQTWVKKLREVIQ 120
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
766-868 1.14e-16

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 76.28  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  766 PNFIQEvapeflvPLVDVTCLLGDTVILQCKVCGRPKPTITWKgpdQNILDTDNSSATYTVsscdsGEITLKICNLMPQD 845
Cdd:cd20978    1 PKFIQK-------PEKNVVVKGGQDVTLPCQVTGVPQPKITWL---HNGKPLQGPMERATV-----EDGTLTIINVQPED 65
                         90       100
                 ....*....|....*....|...
gi 68362740  846 SGIYTCIATNDHGTTSTSATVKV 868
Cdd:cd20978   66 TGYYGCVATNEIGDIYTETLLHV 88
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
992-1190 1.33e-16

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: 81.00  E-value: 1.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    992 EIGRGRFSIVKKCI----HKATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:pfam07714    6 KLGEGAFGEVYKGTlkgeGENTKIKVAVKTLKEGADEEEREDflEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   1066 GRLLDYLMNHDEL--MEEKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFHIH 1141
Cdd:pfam07714   86 GDLLDFLRKHKRKltLKDLLSM-ALQIAKGMEYLESKNFVHRDLAARNCLVSEN---LVVKISDfgLSRDIYDDDYYRKR 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 68362740   1142 -HLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEE 1190
Cdd:pfam07714  162 gGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE 212
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
993-1229 1.40e-16

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: 82.62  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKM-KKKEQAAH---EAALLQHL---QHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKViVAKKEVAHtigERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLE-DAVQISGHFHIHHLL 1144
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDAN---GHIALCDFGlSKADLTDNKTTNTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEV-IQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYfcgVSNAARDFINVILQ 1223
Cdd:cd05586  158 GTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDV---LSDEGRSFVKGLLN 234

                 ....*.
gi 68362740 1224 EDFRRR 1229
Cdd:cd05586  235 RNPKHR 240
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
987-1243 1.63e-16

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: 82.64  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS---KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSY------I 1057
Cdd:cd07879   17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpfQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGdefqdfY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGrlLDYLMNHdELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPVPRVKLIDLEDAvQIS 1135
Cdd:cd07879   97 LVMPYMQTD--LQKIMGH-PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVneDCELKILDFGLARHADA-EMT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHFHIHHllgnpeFAAPEVI-QGIPVSLGTDIWSIGVLTYVMLSGVSPF--------------------------LDESK 1188
Cdd:cd07879  173 GYVVTRW------YRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFkgkdyldqltqilkvtgvpgpefvqkLEDKA 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1189 EETCIN----VCRVDFS--FPHeyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWLQP 1243
Cdd:cd07879  247 AKSYIKslpkYPRKDFStlFPK-----ASPQAVDLLEKMLELDVDKRLTATEALEHPYFDS 302
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
987-1241 1.64e-16

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: 81.59  E-value: 1.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd07871    7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApcTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGrLLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFHIH 1141
Cdd:cd07871   87 SD-LKQYLDNCGNLMSmHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADfgLARAKSVPTKTYSN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 H-----------LLGNPEFAAPeviqgipvslgTDIWSIGVLTYVMLSGVSPF---------------LDESKEETCINV 1195
Cdd:cd07871  163 EvvtlwyrppdvLLGSTEYSTP-----------IDMWGVGCILYEMATGRPMFpgstvkeelhlifrlLGTPTEETWPGV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1196 CRVD----FSFPhEYFCG--VSNAAR------DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07871  232 TSNEefrsYLFP-QYRAQplINHAPRldtdgiDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
993-1242 2.11e-16

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: 80.90  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH------EAALLQHLQHPQ----YITLHDTYESptSYILILEL 1062
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEvsalecEIQLLKNLQHERivqyYGCLRDRAEK--TLTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLE-----DAVQISGH 1137
Cdd:cd06651   93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD---SAGNVKLGDFGaskrlQTICMSGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 fHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfCGVSNAARDF 1217
Cdd:cd06651  170 -GIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLP--SHISEHARDF 246
                        250       260
                 ....*....|....*....|....*
gi 68362740 1218 INVILQEDfRRRPTAATCLQHPWLQ 1242
Cdd:cd06651  247 LGCIFVEA-RHRPSAEELLRHPFAQ 270
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
987-1241 2.78e-16

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: 80.16  E-value: 2.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSK------KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILIL 1060
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEisvgelQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGRLLD----YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlripvpRVKLIDLedavqisG 1136
Cdd:cd08222   82 EYCEGGDLDDkiseYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-------KNNVIKV-------G 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHLL-----------GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF-SFPH 1204
Cdd:cd08222  148 DFGISRILmgtsdlattftGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPD 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 68362740 1205 EYfcgvSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd08222  228 KY----SKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
993-1184 2.84e-16

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: 80.78  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSK--KMKKKEQAAHEAALLQHLQHPQYITLHDTYE-----SPTSY-ILILELMD 1064
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQelSPKNRERWCLEIQIMKRLNHPNVVAARDVPEglqklAPNDLpLLAMEYCQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLmNHDE----LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLidLRIPVPRV--KLIDLEDAVQISGHF 1138
Cdd:cd14038   82 GGDLRKYL-NQFEnccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIV--LQQGEQRLihKIIDLGYAKELDQGS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 68362740 1139 HIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL 1184
Cdd:cd14038  159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
PH_Dbs cd01227
DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming ...
415-531 3.56e-16

DBL's big sister protein pleckstrin homology (PH) domain; Dbs (also called MCF2-transforming sequence-like protein 2) is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a rhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269934 [Multi-domain]  Cd Length: 126  Bit Score: 76.08  E-value: 3.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  415 GFEGTLTAQGKLLQQDTFYV-IELDAG-----MQSRTKERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYLVLEEN 488
Cdd:cd01227    4 GYDGNLGDLGKLLMQGSFNVwTEHKKGhtkklARFKPMQRHIFLYEKAVLFCKKRGENGEAPSYSYKNSLNTTAVGLTEN 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 68362740  489 VDNDPCKFALMNRETSERVVLQAANADIQQAWVQDINQVLETQ 531
Cdd:cd01227   84 VKGDTKKFEIWLNGREEVFIIQAPTPEIKAAWVKAIRQVLLSQ 126
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1065-1245 3.86e-16

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: 82.00  E-value: 3.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLdyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL-------------------RIPVPRVKL 1125
Cdd:cd05600   97 DFRTL--LNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSsghikltdfglasgtlspkKIESMKIRL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1126 IDLEDAVQiSGHFH-----------------IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESK 1188
Cdd:cd05600  175 EEVKNTAF-LELTAkerrniyramrkedqnyANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTP 253
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1189 EETCINVC-------RVDFSFPHEYFcGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHN 1245
Cdd:cd05600  254 NETWANLYhwkktlqRPVYTDPDLEF-NLSDEAWDLITKLITDPQDRLQSPEQIKNHPFFKNID 316
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
987-1240 4.09e-16

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: 80.24  E-value: 4.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIrldTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 --DDGRLLDyLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFH 1139
Cdd:cd07860   82 hqDLKKFMD-ASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTE---GAIKLADfgLARAFGVPVRTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLgNPEFAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV----------------DF-- 1200
Cdd:cd07860  158 THEVV-TLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTlgtpdevvwpgvtsmpDYkp 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1201 SFP-------HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07860  237 SFPkwarqdfSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
987-1241 4.56e-16

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: 80.67  E-value: 4.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCI-HKaTRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHpqyitlHDtyESPTSYILilelmdd 1065
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLdHK-TGQLVAIKIIRNKKRFHQQALVEVKILKHLND------ND--PDDKHNIV------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 gRLLDYL--------------MNHDELME------------EKVAfyiRDIMEALQYLHNCRVAHLDIKPENLLIDLRIP 1119
Cdd:cd14210   79 -RYKDSFifrghlcivfellsINLYELLKsnnfqglslsliRKFA---KQILQALQFLHKLNIIHCDLKPENILLKQPSK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1120 VpRVKLIDLEdavqiSGHFHihhllGNPEFA--------APEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE- 1190
Cdd:cd14210  155 S-SIKVIDFG-----SSCFE-----GEKVYTyiqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEq 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1191 -TCI------------NVCRVDFSF------PHEYFCG---------VSNAAR---------DFINVILQEDFRRRPTAA 1233
Cdd:cd14210  224 lACImevlgvppksliDKASRRKKFfdsngkPRPTTNSkgkkrrpgsKSLAQVlkcddpsflDFLKKCLRWDPSERMTPE 303

                 ....*...
gi 68362740 1234 TCLQHPWL 1241
Cdd:cd14210  304 EALQHPWI 311
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
987-1230 4.92e-16

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: 79.69  E-value: 4.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH-EAALLQHL-QHPQYITLHDT---YESPTSYILILe 1061
Cdd:cd13985    2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIkEIEIMKRLcGHPNIVQYYDSailSSEGRKEVLLL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 lMD--DGRLLDYLMN--HDELMEEKVAFYIRDIMEALQYLHNC--RVAHLDIKPENLLI-DLRipvpRVKLIDL------ 1128
Cdd:cd13985   81 -MEycPGSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFsNTG----RFKLCDFgsatte 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 -------EDAVQISGHFHIHHllgNPEFAAPEVI---QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKeetcINVCRV 1198
Cdd:cd13985  156 hypleraEEVNIIEEEIQKNT---TPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSK----LAIVAG 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1199 DFSFPHEYFCgvSNAARDFINVILQEDFRRRP 1230
Cdd:cd13985  229 KYSIPEQPRY--SPELHDLIRHMLTPDPAERP 258
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1028-1241 4.94e-16

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: 79.40  E-value: 4.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1028 AAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNH-DELM-EEKVAFYIRDIMEALQYLHNCRVAHL 1105
Cdd:cd08221   46 ALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQkNQLFpEEVVLWYLYQIVSAVSHIHKAGILHR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1106 DIKPENLLI---DLripvprVKLIDLEDAVQISGHFHI-HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVS 1181
Cdd:cd08221  126 DIKTLNIFLtkaDL------VKLGDFGISKVLDSESSMaESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKR 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1182 PFLDESKEETCINVCRVDFSFPHEYFcgvSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd08221  200 TFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
987-1239 4.96e-16

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: 80.24  E-value: 4.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVskkmkkkEQAAH----EAALLQHLQHPQYITLHDTYESPTS------Y 1056
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV-------LQDKRyknrELQIMRRLKHPNIVKLKYFFYSSGEkkdevyL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDgRLLDYLMNHDELMEEKVAFYIRDIM----EALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAV 1132
Cdd:cd14137   79 NLVMEYMPE-TLYRVIRHYSKNKQTIPIIYVKLYSyqlfRGLAYLHSLGICHRDIKPQNLLVDPETGV--LKLCDFGSAK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1133 QIsghfhihhLLGNPEFA--------APEVIQGIP---VSLgtDIWSIG-VLTYVML--------SGV-----------S 1181
Cdd:cd14137  156 RL--------VPGEPNVSyicsryyrAPELIFGATdytTAI--DIWSAGcVLAELLLgqplfpgeSSVdqlveiikvlgT 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1182 PfldeSKEE-TCINVCRVDFSFPHEYFCGVSNA--------ARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd14137  226 P----TREQiKAMNPNYTEFKFPQIKPHPWEKVfpkrtppdAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
981-1244 5.46e-16

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: 80.81  E-value: 5.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS--KKMKKKEQAAHEAALLQHLQHPQYITLHD-----TYESP 1053
Cdd:cd07849    1 FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCLRTLREIKILLRFKHENIIGILDiqrppTFESF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMD-DgrlLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLRIpvprvklIDL 1128
Cdd:cd07849   81 KDVYIVQELMEtD---LYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLntncDLKI-------CDF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDA-VQISGHFHIHHLLgnpEFA------APEVI---QGIPVSLgtDIWSIGVLTYVMLSGVSPF-----LDE------- 1186
Cdd:cd07849  151 GLArIADPEHDHTGFLT---EYVatrwyrAPEIMlnsKGYTKAI--DIWSVGCILAEMLSNRPLFpgkdyLHQlnlilgi 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1187 ----SKEE-TCINVCRV-DF--SFPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd07849  226 lgtpSQEDlNCIISLKArNYikSLPFkpkvpwnKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQY 298
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
983-1244 6.28e-16

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: 80.49  E-value: 6.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSY--- 1056
Cdd:cd07855    3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRtlrELKILRHFKHDNIIAIRDILRPKVPYadf 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ---ILILELMDDGrlLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLID----LRIPvprvkliDL 1128
Cdd:cd07855   83 kdvYVVLDLMESD--LHHIIHSDQpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNenceLKIG-------DF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQISG------HFHIHHLLGNPeFAAPEVIQGIP-VSLGTDIWSIGVL--------------TYV----MLSGV--S 1181
Cdd:cd07855  154 GMARGLCTspeehkYFMTEYVATRW-YRAPELMLSLPeYTQAIDMWSVGCIfaemlgrrqlfpgkNYVhqlqLILTVlgT 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1182 P---FLDESKEE---TCINvcrvdfSFP-------HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd07855  233 PsqaVINAIGADrvrRYIQ------NLPnkqpvpwETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKY 302
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
993-1229 6.30e-16

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: 80.48  E-value: 6.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQH---PQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd14223    8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSFILDLMNG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHfHIHHLLG 1145
Cdd:cd14223   88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEF---GHVRISDLGLACDFSKK-KPHASVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQ-GIPVSLGTDIWSIGVLTYVMLSGVSPFlDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQE 1224
Cdd:cd14223  164 THGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPF-RQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQR 242

                 ....*
gi 68362740 1225 DFRRR 1229
Cdd:cd14223  243 DVNRR 247
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
987-1240 6.50e-16

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: 79.92  E-value: 6.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQHPQYITLHDTYESP------TSYI 1057
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGfpiTAIREIKLLQKLDHPNVVRLKEIVTSKgsakykGSIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMD-DgrlLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQI 1134
Cdd:cd07840   81 MVFEYMDhD---LTGLLDNPEvkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND---GVLKLADFGLARPY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1135 SGHfhihhllGNPEFA---------APEVIqgipvsLGT-------DIWSIGVLTYVMLSGvSPFL---DESKEETCI-N 1194
Cdd:cd07840  155 TKE-------NNADYTnrvitlwyrPPELL------LGAtrygpevDMWSVGCILAELFTG-KPIFqgkTELEQLEKIfE 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1195 VC--------------------RVDFSFPH---EYFCGV-SNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07840  221 LCgspteenwpgvsdlpwfenlKPKKPYKRrlrEVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
993-1184 9.15e-16

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: 79.41  E-value: 9.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVK----FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYE-----SPTSY-ILILEL 1062
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPeleklSPNDLpLLAMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYL---MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVP-RV--KLIDLEDAVQISG 1136
Cdd:cd13989   81 CSGGDLRKVLnqpENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQ---QGGgRViyKLIDLGYAKELDQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1137 HFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL 1184
Cdd:cd13989  158 GSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL 205
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
993-1234 9.60e-16

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: 79.20  E-value: 9.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKAtrKDVAVKF----------------------VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTY 1050
Cdd:cd14000    2 LGDGGFGSVYRASYKG--EPVAVKIfnkhtssnfanvpadtmlrhlrATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1051 ESPTsyILILELMDDGRLlDYLMNHDE--------LMEEKVAFYIRDimeALQYLHNCRVAHLDIKPENLLIdLRIPVPR 1122
Cdd:cd14000   80 IHPL--MLVLELAPLGSL-DHLLQQDSrsfaslgrTLQQRIALQVAD---GLRYLHSAMIIYRDLKSHNVLV-WTLYPNS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1123 VKLIDLED--AVQISGHFHIHHLLGNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVD 1199
Cdd:cd14000  153 AIIIKIADygISRQCCRMGAKGSEGTPGFRAPEIARGnVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGL 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 68362740 1200 FSFPHEYFCGVSNAARDFINVILQEDFRRRPTAAT 1234
Cdd:cd14000  233 RPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVT 267
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
993-1239 1.01e-15

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: 78.63  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVS-------KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcrnsssEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlrIPVPRVKLIDLEDAVQIS------GHFH 1139
Cdd:cd06630   88 GSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVD--STGQRLRIADFGAAARLAskgtgaGEFQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 iHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFldeskeetciNVCRVDFSF-----------PHEYFC 1208
Cdd:cd06630  166 -GQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW----------NAEKISNHLalifkiasattPPPIPE 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 68362740 1209 GVSNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd06630  235 HLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
990-1242 1.07e-15

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: 79.31  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd06644   17 IGELGDGAFGKVYKAKNKETGALAAAKVIeTKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI---------DLRIPVPRVKLIDLEDAvqisghf 1138
Cdd:cd06644   97 DAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLtldgdiklaDFGVSAKNVKTLQRRDS------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 hihhLLGNPEFAAPEVI-----QGIPVSLGTDIWSIGVlTYVMLSGVSPFLDE-SKEETCINVCRVD---FSFPHEYfcg 1209
Cdd:cd06644  170 ----FIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGI-TLIEMAQIEPPHHElNPMRVLLKIAKSEpptLSQPSKW--- 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 68362740 1210 vSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06644  242 -SMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
987-1242 1.47e-15

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: 79.61  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK-----FVSKKMKkkEQAAHEAALLQHLQHPQYITLHDTYESPTS------ 1055
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKklyrpFQSELFA--KRAYRELRLLKHMKHENVIGLLDVFTPDLSldrfhd 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILILELMddGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQIS 1135
Cdd:cd07880   95 FYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDC---ELKILDFGLARQTD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GhfHIHHLLGNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGV-SNA 1213
Cdd:cd07880  170 S--EMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLqSED 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1214 ARDFINVI---LQEDFR-----------------------RRPTAATCLQHPWLQ 1242
Cdd:cd07880  248 AKNYVKKLprfRKKDFRsllpnanplavnvlekmlvldaeSRITAAEALAHPYFE 302
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1039-1242 1.58e-15

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: 79.58  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1039 QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRi 1118
Cdd:cd05619   64 EHPFLTHLFCTFQTKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKD- 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1119 pvPRVKLIDLEDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVcR 1197
Cdd:cd05619  143 --GHIKIADFGMCKEnMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI-R 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 68362740 1198 VDFSFpheYFCGVSNAARD-FINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd05619  220 MDNPF---YPRWLEKEAKDiLVKLFVREPERRLGVRGDIRQHPFFR 262
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
987-1241 1.61e-15

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: 78.34  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK-----FVSKkmkkkeqaaHEAALLQHLQ-------HPQYITLHDTY-ESP 1053
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKkmkkkFYSW---------EECMNLREVKslrklneHPNIVKLKEVFrEND 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYiLILELMDdGRLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDA 1131
Cdd:cd07830   72 ELY-FVFEYME-GNLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 vqisghfhiHHLLGNPEFA---------APEVI-----QGIPVslgtDIWSIGVLTYVMLSGVSPF-----LDE------ 1186
Cdd:cd07830  147 ---------REIRSRPPYTdyvstrwyrAPEILlrstsYSSPV----DIWALGCIMAELYTLRPLFpgsseIDQlykics 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1187 -----SKE---ETCINVCRVDFSFP-------HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07830  214 vlgtpTKQdwpEGYKLASKLGFRFPqfaptslHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
993-1232 2.37e-15

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: 77.78  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--------AAHEAALLQHL-QHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDgndfqklpQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEYC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMN--HDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipVPRVKLIDLEDAVQ--ISGHFH 1139
Cdd:cd13993   88 PNGDLFEAITEnrIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQD--EGTVKLCDFGLATTekISMDFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IhhllGNPEFAAPEVIQGIPVSLGT------DIWSIGVLTYVMLSGVSPFLDESKEEtcINVCRVDFSFPHeYFCGVSNA 1213
Cdd:cd13993  166 V----GSEFYMAPECFDEVGRSLKGypcaagDIWSLGIILLNLTFGRNPWKIASESD--PIFYDYYLNSPN-LFDVILPM 238
                        250       260
                 ....*....|....*....|..
gi 68362740 1214 ARDFINV---ILQEDFRRRPTA 1232
Cdd:cd13993  239 SDDFYNLlrqIFTVNPNNRILL 260
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
987-1241 2.50e-15

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: 78.10  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIrleTEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 D-DgrlLDYLMNH---DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGH 1137
Cdd:cd07835   81 DlD---LKKYMDSsplTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTE---GALKLADfgLARAFGVPVR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLLgNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV----------------DF 1200
Cdd:cd07835  155 TYTHEVV-TLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTlgtpdedvwpgvtslpDY 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740 1201 --SFP-------HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07835  234 kpTFPkwarqdlSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
987-1170 3.43e-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: 78.45  E-value: 3.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQhlqhpqyiTLHDTYESPTSYILIlelmddg 1066
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILT--------LLNTKYDPEDKHHIV------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHD--------------ELMEEK---------VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIPVPRV 1123
Cdd:cd14212   66 RLLDHFMHHGhlcivfellgvnlyELLKQNqfrglslqlIRKFLQQLLDALSVLKDARIIHCDLKPENILLV-NLDSPEI 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1124 KLIDLEDA----------VQiSGHFHihhllgnpefaAPEVIQGIPVSLGTDIWSIG 1170
Cdd:cd14212  145 KLIDFGSAcfenytlytyIQ-SRFYR-----------SPEVLLGLPYSTAIDMWSLG 189
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
991-1183 3.70e-15

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: 76.81  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVKKCIHK---ATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKggdGKTVDVAVKTLKEDASESERKDflKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDEL----------MEEKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQIS 1135
Cdd:cd00192   81 GDLLDFLRKSRPVfpspepstlsLKDLLSF-AIQIAKGMEYLASKKFVHRDLAARNCLVGED---LVVKISDFGLSRDIY 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1136 GHFHIHHLLGNPE---FAAPEVIQ-GIpVSLGTDIWSIGVLTYVMLS-GVSPF 1183
Cdd:cd00192  157 DDDYYRKKTGGKLpirWMAPESLKdGI-FTSKSDVWSFGVLLWEIFTlGATPY 208
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
993-1183 4.49e-15

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: 77.85  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL-----QHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVfetasNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID-------LEDAvQISGHFhi 1140
Cdd:cd05588   83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSE---GHIKLTDygmckegLRPG-DTTSTF-- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1141 hhlLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd05588  157 ---CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
774-855 4.81e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 71.44  E-value: 4.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSATYtvsscDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSL-----SGSNSTLTISNVTRSDAGTYTCVA 76

                   ..
gi 68362740    854 TN 855
Cdd:pfam13927   77 SN 78
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
988-1252 5.03e-15

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: 77.08  E-value: 5.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  988 TELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAheaaLLQHLQ-------HPQYITLHDTYESPTSYILIL 1060
Cdd:cd06617    4 EVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKR----LLMDLDismrsvdCPYTVTFYGALFREGDVWICM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGrlLDYL----MNHDELMEE----KVAFyirDIMEALQYLH-NCRVAHLDIKPENLLIDLRipvPRVKLIDLeda 1131
Cdd:cd06617   80 EVMDTS--LDKFykkvYDKGLTIPEdilgKIAV---SIVKALEYLHsKLSVIHRDVKPSNVLINRN---GQVKLCDF--- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 vQISGHFhIHHL-----LGNPEFAAPEVI------QGIPVSlgTDIWSIGVLTYVMLSGVSPF---------LDESKEET 1191
Cdd:cd06617  149 -GISGYL-VDSVaktidAGCKPYMAPERInpelnqKGYDVK--SDVWSLGITMIELATGRFPYdswktpfqqLKQVVEEP 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1192 CInvcrvdfSFPHEYFcgvSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHNGSYSKIP 1252
Cdd:cd06617  225 SP-------QLPAEKF---SPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVA 275
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
993-1238 5.37e-15

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: 76.59  E-value: 5.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK----EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd14188    9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqrEKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHFHIHHLL-GNP 1147
Cdd:cd14188   89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENM---ELKVGDFGLAARLEPLEHRRRTIcGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEET--CINVCRvdFSFPHEyfcgVSNAARDFINVILQED 1225
Cdd:cd14188  166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETyrCIREAR--YSLPSS----LLAPAKHLIASMLSKN 239
                        250
                 ....*....|...
gi 68362740 1226 FRRRPTAATCLQH 1238
Cdd:cd14188  240 PEDRPSLDEIIRH 252
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
987-1240 6.43e-15

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: 76.75  E-value: 6.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIhlDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 dGRLLDYLMNHDE---LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDledavqisghFHIH 1141
Cdd:cd07836   82 -KDLKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKR---GELKLAD----------FGLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNPE-----------FAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV-----DFSFPH 1204
Cdd:cd07836  148 RAFGIPVntfsnevvtlwYRAPDVLLGSRTySTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRImgtptESTWPG 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1205 -----EY---------------FCGVSNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07836  228 isqlpEYkptfpryppqdlqqlFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
994-1183 8.35e-15

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: 75.38  E-value: 8.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  994 GRGRFSIVKKCIHKATRKDVAVKFVSkkmkkkeQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLM 1073
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLL-------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1074 NHD--ELMEEKVAFYIRDIMEALQYLHN---CRVAHLDIKPENLLIDLRIPVprvKLIDLeDAVQISGHFHIHHLLGNPE 1148
Cdd:cd14060   75 SNEseEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVL---KICDF-GASRFHSHTTHMSLVGTFP 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 68362740 1149 FAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14060  151 WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
987-1241 8.78e-15

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: 76.10  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIhKATRKDVAVKFVSKKMKKkEQAAH----EAALLQHLQH-PQYITLHDtYE--SPTSYILI 1059
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGAD-EQTLQsyknEIELLKKLKGsDRIIQLYD-YEvtDEDDYLYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlripVP-RVKLIDLEDAVQI-S 1135
Cdd:cd14131   80 VMECGEIDLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-----VKgRLKLIDFGIAKAIqN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHFHIH--HLLGNPEFAAPEVIQG----------IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDF 1200
Cdd:cd14131  155 DTTSIVrdSQVGTLNYMSPEAIKDtsasgegkpkSKIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAIidpNHEI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 68362740 1201 SFPheyfcgvSNAARDFINVI---LQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14131  235 EFP-------DIPNPDLIDVMkrcLQRDPKKRPSIPELLNHPFL 271
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
993-1183 1.08e-14

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: 77.37  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL-----QHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05617   23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVfeqasSNPFLVGLHSCFQTTSRLFLVIEYVNGGD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHLLGN 1146
Cdd:cd05617  103 LMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDAD---GHIKLTDYGMCKEgLGPGDTTSTFCGT 179
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd05617  180 PNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
993-1275 1.22e-14

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: 77.20  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVK-FVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05629    9 IGKGAFGEVRLVQKKDTGKIYAMKtLLKSEMFKKDQLAHvkaERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLedavQISGHFHIHH------ 1142
Cdd:cd05629   89 MTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRG---GHIKLSDF----GLSTGFHKQHdsayyq 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 ----------------------------------------------LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVM 1176
Cdd:cd05629  162 kllqgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaysTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFEC 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1177 LSGVSPFLDESKEETC--INVCRVDFSFPHEYFCGVSnaARDFINVILQEDFRR--RPTAATCLQHPWlqphngsYSKIP 1252
Cdd:cd05629  242 LIGWPPFCSENSHETYrkIINWRETLYFPDDIHLSVE--AEDLIRRLITNAENRlgRGGAHEIKSHPF-------FRGVD 312
                        330       340
                 ....*....|....*....|....*
gi 68362740 1253 LDTSRL--ACFIERRKHQNDVRPIP 1275
Cdd:cd05629  313 WDTIRQirAPFIPQLKSITDTSYFP 337
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
990-1241 1.36e-14

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: 75.66  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG- 1066
Cdd:cd06622    6 LDELGKGNYGSVYKVLHRPTGVTMAMKEIrlELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 --RLLDYLMNHDELMEEKVAFYIRDIMEALQYL---HNcrVAHLDIKPENLLIDLRipvPRVKLIDLedavQISGHFhIH 1141
Cdd:cd06622   86 ldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVNGN---GQVKLCDF----GVSGNL-VA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HL----LGNPEFAAPEVIQ-GIPVSLGT-----DIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVS 1211
Cdd:cd06622  156 SLaktnIGCQSYMAPERIKsGGPNQNPTytvqsDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLPSGYS 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 68362740 1212 NAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06622  236 DDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
990-1183 1.57e-14

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: 77.00  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL-----QHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05618   25 LRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVfeqasNHPFLVGLHSCFQTESRLFFVIEYVN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHL 1143
Cdd:cd05618  105 GGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE---GHIKLTDYGMCKEgLRPGDTTSTF 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd05618  182 CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
993-1252 1.85e-14

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: 76.46  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKK----MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKAdminKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLID------------LRIPVPR-VKLIDL------- 1128
Cdd:cd05610   92 KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISneghikltdfglSKVTLNReLNMMDIlttpsma 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 ---EDAVQISGHFH--IHHL--------------------------LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVML 1177
Cdd:cd05610  172 kpkNDYSRTPGQVLslISSLgfntptpyrtpksvrrgaarvegeriLGTPDYLAPELLLGKPHGPAVDWWALGVCLFEFL 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1178 SGVSPFLDESKEETCINVCRVDFSFPHEYFcGVSNAARDFINVILQEDFRRRPTAATCLQHP------WLQPHNGSYSKI 1251
Cdd:cd05610  252 TGIPPFNDETPQQVFQNILNRDIPWPEGEE-ELSVNAQNAIEILLTMDPTKRAGLKELKQHPlfhgvdWENLQNQTMPFI 330

                 .
gi 68362740 1252 P 1252
Cdd:cd05610  331 P 331
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
985-1283 1.87e-14

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: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS-------- 1055
Cdd:cd07854    5 SRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVlTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGSdltedvgs 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 -------YIlILELMDDGrlLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDL 1128
Cdd:cd07854   85 ltelnsvYI-VQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLV--LKIGDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQISGHF-HIHHL---LGNPEFAAPE-VIQGIPVSLGTDIWSIGVLTYVMLSGVS------------------PFLD 1185
Cdd:cd07854  160 GLARIVDPHYsHKGYLsegLVTKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPlfagaheleqmqlilesvPVVR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1186 ESKEETCINV----CRVDFSFPH----EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPhngsYSkIPLD--T 1255
Cdd:cd07854  240 EEDRNELLNVipsfVRNDGGEPRrplrDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSC----YS-CPFDepV 314
                        330       340
                 ....*....|....*....|....*...
gi 68362740 1256 SRLACFIErrKHQNDVRPIPNVKSYIVN 1283
Cdd:cd07854  315 SLHPFHIE--DELDDILLMTEIHSIIYN 340
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
990-1254 2.15e-14

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: 76.06  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHL-QHPQYITLHDTY--ESPTSYILILELM 1063
Cdd:cd07852   12 LKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRtfrEIMFLQELnDHPNIIKLLNVIraENDKDIYLVFEYM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 D-DgrlLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGhfhihh 1142
Cdd:cd07852   92 EtD---LHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDC---RVKLADFGLARSLSQ------ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFA------------APEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPF-----LDE-----------SKEEtcI 1193
Cdd:cd07852  160 LEEDDENPvltdyvatrwyrAPEILLGSTrYTKGVDMWSVGCILGEMLLGKPLFpgtstLNQlekiievigrpSAED--I 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1194 NVCRVDFS-------------FPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQP-HNGS-------YSKIP 1252
Cdd:cd07852  238 ESIQSPFAatmleslppsrpkSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQfHNPAdepslpgPIVIP 317

                 ..
gi 68362740 1253 LD 1254
Cdd:cd07852  318 LD 319
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
1013-1185 2.16e-14

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: 74.07  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1013 VAVKFVSkkmkkkEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIME 1092
Cdd:cd14059   19 VAVKKVR------DEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIAS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1093 ALQYLHNCRVAHLDIKPENLLI---DLripvprVKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSI 1169
Cdd:cd14059   93 GMNYLHLHKIIHRDLKSPNVLVtynDV------LKISDFGTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSF 166
                        170
                 ....*....|....*.
gi 68362740 1170 GVLTYVMLSGVSPFLD 1185
Cdd:cd14059  167 GVVLWELLTGEIPYKD 182
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
973-1242 2.18e-14

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: 75.84  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  973 DGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHD 1048
Cdd:cd06633    9 EIADLFYKDDPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwqdiIKEVKFLQQLKHPNTIEYKG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1049 TYESPTSYILILELMdDGRLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLidLRIPvPRVKLID 1127
Cdd:cd06633   89 CYLKDHTAWLVMEYC-LGSASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNIL--LTEP-GQVKLAD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1128 LEDAVQISGhfhIHHLLGNPEFAAPEVIQGI---PVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDfsFPH 1204
Cdd:cd06633  165 FGSASIASP---ANSFVGTPYWMAPEVILAMdegQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SPT 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 68362740 1205 EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06633  240 LQSNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR 277
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
987-1170 2.18e-14

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: 75.84  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP-----QYITLHDTYESPTSYILILE 1061
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNEnadefNFVRAYECFQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGrLLDYL-MNHDELMEEKVafyIRDIME----ALQYLHNCRVAHLDIKPEN-LLID-LRIPVpRVKLIDLEDAVQI 1134
Cdd:cd14229   82 MLEQN-LYDFLkQNKFSPLPLKV---IRPILQqvatALKKLKSLGLIHADLKPENiMLVDpVRQPY-RVKVIDFGSASHV 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 68362740 1135 SGHFhIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIG 1170
Cdd:cd14229  157 SKTV-CSTYLQSRYYRAPEIILGLPFCEAIDMWSLG 191
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
1013-1241 2.36e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 76.17  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1013 VAVK-FVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIR 1088
Cdd:PTZ00426   59 VAIKrFEKSKIIKQKQVDHvfsERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1089 DIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGhfHIHHLLGNPEFAAPEVIQGIPVSLGTDIWS 1168
Cdd:PTZ00426  139 QIVLIFEYLQSLNIVYRDLKPENLLLDKD---GFIKMTDFGFAKVVDT--RTYTLCGTPEYIAPEILLNVGHGKAADWWT 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740  1169 IGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQEDFRRR-----PTAATCLQHPWL 1241
Cdd:PTZ00426  214 LGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPK----FLDNNCKHLMKKLLSHDLTKRygnlkKGAQNVKEHPWF 287
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
782-868 2.64e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 69.46  E-value: 2.64e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     782 DVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNssaTYTVSScDSGEITLKICNLMPQDSGIYTCIATNDHGTTS 861
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG---RFSVSR-SGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                    ....*..
gi 68362740     862 TSATVKV 868
Cdd:smart00410   79 SGTTLTV 85
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
987-1240 3.22e-14

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: 74.77  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK-FVSKKMKKK--EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKkFLESEDDKMvkKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDgRLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIH- 1141
Cdd:cd07846   83 DH-TVLDDLEKYPNgLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAAPGEVYt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLLGNPEFAAPEVIQGIPvSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETC--INVCRVDFSFPHE-------YFCGV 1210
Cdd:cd07846  159 DYVATRWYRAPELLVGDT-KYGkaVDVWAVGCLVTEMLTGEPLFPGDSDIDQLyhIIKCLGNLIPRHQelfqknpLFAGV 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1211 ------------------SNAARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07846  238 rlpevkeveplerrypklSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
993-1229 3.32e-14

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: 75.48  E-value: 3.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQH---PQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05633   13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLCFILDLMNG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHfHIHHLLG 1145
Cdd:cd05633   93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEH---GHVRISDLGLACDFSKK-KPHASVG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVIQ-GIPVSLGTDIWSIGVLTYVMLSGVSPFLD---ESKEETCINVCRVDFSFPHEYfcgvSNAARDFINVI 1221
Cdd:cd05633  169 THGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFRQhktKDKHEIDRMTLTVNVELPDSF----SPELKSLLEGL 244

                 ....*...
gi 68362740 1222 LQEDFRRR 1229
Cdd:cd05633  245 LQRDVSKR 252
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
986-1183 3.40e-14

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: 74.61  E-value: 3.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07870    1 SYLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVpfTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGrLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLripVPRVKLID--LEDAVQISGHFHI 1140
Cdd:cd07870   81 HTD-LAQYMIQHpGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISY---LGELKLADfgLARAKSIPSQTYS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 68362740 1141 HHLLgNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd07870  157 SEVV-TLWYRPPDVLLGaTDYSSALDIWGAGCIFIEMLQGQPAF 199
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
992-1183 3.41e-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: 74.27  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVA---VKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS----YILILELMD 1064
Cdd:cd14033    8 EIGRGSFKTVYRGLDTETTVEVAwceLQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHN--CRVAHLDIKPENLLIDLriPVPRVKLIDLEDAVQISGHFhIHH 1142
Cdd:cd14033   88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrcPPILHRDLKCDNIFITG--PTGSVKIGDLGLATLKRASF-AKS 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1143 LLGNPEFAAPEVIQGiPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14033  165 VIGTPEFMAPEMYEE-KYDEAVDVYAFGMCILEMATSEYPY 204
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
987-1128 3.57e-14

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 74.03  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKeQAAHEAALLQHLQHPQYI-TLHDTYESPTSYILILELMdd 1065
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHP-QLEYEAKVYKLLQGGPGIpRLYWFGQEGDYNVMVMDLL-- 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1066 GRLLDYLMN-HDELMEEKVAFYIRDIM-EALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDL 1128
Cdd:cd14016   79 GPSLEDLFNkCGRKFSLKTVLMLADQMiSRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDF 143
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
872-954 3.58e-14

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 3.58e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     872 PAAPNRPIAQERSCTSVILRWLPPSSTGNCT-ISGYTVEYREEGSQiWQQSVASTLDTYLVIEDLSPGCPYQFRVSASNP 950
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYREEGSE-WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 68362740     951 WGIS 954
Cdd:smart00060   80 AGEG 83
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
985-1219 5.40e-14

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: 75.13  E-value: 5.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP-----QYITLHDTYESPTSYILI 1059
Cdd:cd14228   15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSEnadeyNFVRSYECFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDgRLLDYL-MNHDELMEEKvafYIRDIME----ALQYLHNCRVAHLDIKPENLLIDLRIPVP-RVKLIDLEDAVQ 1133
Cdd:cd14228   95 FEMLEQ-NLYDFLkQNKFSPLPLK---YIRPILQqvatALMKLKSLGLIHADLKPENIMLVDPVRQPyRVKVIDFGSASH 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGHFhIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGvSPFLDESKEETCINVCRVDFSFPHEYFCGVSNA 1213
Cdd:cd14228  171 VSKAV-CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASEYDQIRYISQTQGLPAEYLLSAGTK 248

                 ....*.
gi 68362740 1214 ARDFIN 1219
Cdd:cd14228  249 TSRFFN 254
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
1011-1239 5.75e-14

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 73.46  E-value: 5.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1011 KDVAVK-----FVSKkmkkkeqAAHEAALLQHL-QHPQYITLHDTYESPTSYILILELMDdGRLLDYLMNHDELMEEKVA 1084
Cdd:cd13982   26 RPVAVKrllpeFFDF-------ADREVQLLRESdEHPNVIRYFCTEKDRQFLYIALELCA-ASLQDLVESPRESKLFLRP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1085 FY-----IRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPV--PRVKLID------LEDAVQISghFHIHHLLGNPEFAA 1151
Cdd:cd13982   98 GLepvrlLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHgnVRAMISDfglckkLDVGRSSF--SRRSGVAGTSGWIA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1152 PEVIQGIP---VSLGTDIWSIGVLTYVMLS-GVSPFLDESKEETciNVCRVDFSFPHEYFCGVSNA-ARDFINVILQEDF 1226
Cdd:cd13982  176 PEMLSGSTkrrQTRAVDIFSLGCVFYYVLSgGSHPFGDKLEREA--NILKGKYSLDKLLSLGEHGPeAQDLIERMIDFDP 253
                        250
                 ....*....|...
gi 68362740 1227 RRRPTAATCLQHP 1239
Cdd:cd13982  254 EKRPSAEEVLNHP 266
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
993-1241 5.95e-14

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: 73.89  E-value: 5.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYI-TLHDTY--ESPTSY----ILILELMDD 1065
Cdd:cd06636   24 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIaTYYGAFikKSPPGHddqlWLVMEFCGA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF-HIHH 1142
Cdd:cd06636  104 GSVTDLVKNTkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRTVgRRNT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQ-----GIPVSLGTDIWSIGVLTYVMLSGVSPFLDeskeetcINVCRVDFSFPHEYFCGV-----SN 1212
Cdd:cd06636  181 FIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD-------MHPMRALFLIPRNPPPKLkskkwSK 253
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06636  254 KFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
992-1183 6.64e-14

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: 73.60  E-value: 6.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVA-VKFVSKKMKKKEQA--AHEAALLQHLQHPQYITLHDTYES----PTSYILILELMD 1064
Cdd:cd14031   17 ELGRGAFKTVYKGLDTETWVEVAwCELQDRKLTKAEQQrfKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR--VAHLDIKPENLLIDLriPVPRVKLIDLEDAVQISGHFhIHH 1142
Cdd:cd14031   97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG--PTGSVKIGDLGLATLMRTSF-AKS 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1143 LLGNPEFAAPEVIQGiPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14031  174 VIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLEMATSEYPY 213
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
993-1186 6.84e-14

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: 73.26  E-value: 6.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKAllkEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLmnHDELMEEKVAFYIRDIMEA---LQYLHNCR--VAHLDIKPENLLIDLRIpvpRVKLIDLEDAVqISGHFHIHH-- 1142
Cdd:cd13978   81 SLL--EREIQDVPWSLRFRIIHEIalgMNFLHNMDppLLHHDLKPENILLDNHF---HVKISDFGLSK-LGMKSISANrr 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1143 -----LLGNPEFAAPEVI---QGIPvSLGTDIWSIGVLTYVMLSGVSPFLDE 1186
Cdd:cd13978  155 rgtenLGGTPIYMAPEAFddfNKKP-TSKSDVYSFAIVIWAVLTRKEPFENA 205
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
993-1229 6.97e-14

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: 73.63  E-value: 6.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQH----PQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetlALNERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFILDLMN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHfHIHHLL 1144
Cdd:cd05606   82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLD---EHGHVRISDLGLACDFSKK-KPHASV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1145 GNPEFAAPEVIQ-GIPVSLGTDIWSIGVLTYVMLSGVSPFLD---ESKEETCINVCRVDFSFPHEYfcgvSNAARDFINV 1220
Cdd:cd05606  158 GTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQhktKDKHEIDRMTLTMNVELPDSF----SPELKSLLEG 233

                 ....*....
gi 68362740 1221 ILQEDFRRR 1229
Cdd:cd05606  234 LLQRDVSKR 242
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
987-1239 7.18e-14

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 74.12  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVskKMKKKEQAAHEAALLQHLQ-HPQYITLHDT--YESPTSYILILELM 1063
Cdd:cd14132   20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL--KPVKKKKIKREIKILQNLRgGPNIVKLLDVvkDPQSKTPSLIFEYV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 D--DGRLLDYLMNhdelmEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlrIPVPRVKLID--LEDavqisghFH 1139
Cdd:cd14132   98 NntDFKTLYPTLT-----DYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMID--HEKRKLRLIDwgLAE-------FY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLGNPE-----FAAPEVIQGIPV---SLgtDIWSIGVLTYVMLSGVSPF---------------------------- 1183
Cdd:cd14132  164 HPGQEYNVRvasryYKGPELLVDYQYydySL--DMWSLGCMLASMIFRKEPFfhghdnydqlvkiakvlgtddlyayldk 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1184 ----LDESKEETCINVCRVDFS--FPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd14132  242 ygieLPPRLNDILGRHSKKPWErfVNSENQHLVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
993-1183 7.24e-14

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: 72.85  E-value: 7.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKAtrKDVAVKFVsKKMKKKEQAAHEAALLQHLQHPQYITLHD--TYESPTSyiLILELMDDGRLLD 1070
Cdd:cd14058    1 VGRGSFGVVCKARWRN--QIVAVKII-ESESEKKAFEVEVRQLSRVDHPNIIKLYGacSNQKPVC--LVMEYAEGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDELMEEKVAFYIR---DIMEALQYLHNCR---VAHLDIKPENLLIDLRIPVprVKLIDLEDAVQIsgHFHIHHLL 1144
Cdd:cd14058   76 VLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTV--LKICDFGTACDI--STHMTNNK 151
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 68362740 1145 GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14058  152 GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
987-1256 7.43e-14

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: 74.69  E-value: 7.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSyiliLELM 1063
Cdd:cd07877   19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRtyrELRLLKHMKHENVIGLLDVFTPARS----LEEF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHD--------ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDL----EDA 1131
Cdd:cd07877   95 NDVYLVTHLMGADlnnivkcqKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDC---ELKILDFglarHTD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 VQISGHfhihhlLGNPEFAAPEV-IQGIPVSLGTDIWSIGVLTYVMLSGVSPF-----------------------LDES 1187
Cdd:cd07877  172 DEMTGY------VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFpgtdhidqlklilrlvgtpgaelLKKI 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1188 KEETCINVCRVDFSFPH----EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL-QPHNGSYSKI--PLDTS 1256
Cdd:cd07877  246 SSESARNYIQSLTQMPKmnfaNVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFaQYHDPDDEPVadPYDQS 321
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
993-1234 7.94e-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: 73.06  E-value: 7.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKatRKDVAVKFVSKKMKKkEQAAHEAALLQHLQHPQYITLHDTYESPTsyILILELMDDGRLlDYL 1072
Cdd:cd14068    2 LGDGGFGSVYRAVYR--GEDVAVKIFNKHTSF-RLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSL-DAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDE-----LMEEKVAFYIRDimeALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd14068   76 LQQDNasltrTLQHRIALHVAD---GLRYLHSAMIIYRDLKPHNvLLFTLYPNCAIIAKIADYGIAQYCCRMGIKTSEGT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP---HEYFCGVSNAARDFINVIL 1222
Cdd:cd14068  153 PGFRAPEVARGnVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPdpvKEYGCAPWPGVEALIKDCL 232
                        250
                 ....*....|..
gi 68362740 1223 QEDFRRRPTAAT 1234
Cdd:cd14068  233 KENPQCRPTSAQ 244
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
990-1205 8.11e-14

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: 73.49  E-value: 8.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKK---KEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd07848    6 LGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENeevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 rLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQIS--GHFHIHHL 1143
Cdd:cd07848   86 -MLELLEEMpNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHN---DVLKLCDFGFARNLSegSNANYTEY 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHE 1205
Cdd:cd07848  162 VATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAE 223
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
993-1184 8.72e-14

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: 73.41  E-value: 8.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKF--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYI-----LILELMDD 1065
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKScrLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYCSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDyLMNHDE----LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIH 1141
Cdd:cd14039   81 GDLRK-LLNKPEnccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQGSLCT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1142 HLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL 1184
Cdd:cd14039  160 SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFL 202
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
987-1242 9.38e-14

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: 72.87  E-value: 9.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHDTYESPTSYILILEL 1062
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwqdiIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDdGRLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIpvprVKLIDLEDAVQISGhfhI 1140
Cdd:cd06607   83 CL-GSASDIVEVHkKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNiLLTEPGT----VKLADFGSASLVCP---A 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVIQGI---PVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDfsFPHEYFCGVSNAARDF 1217
Cdd:cd06607  155 NSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND--SPTLSSGEWSDDFRNF 232
                        250       260
                 ....*....|....*....|....*
gi 68362740 1218 INVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06607  233 VDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
993-1244 1.02e-13

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: 73.21  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYI-TLHDTY--ESP----TSYILILELMDD 1065
Cdd:cd06637   14 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIaTYYGAFikKNPpgmdDQLWLVMEFCGA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF-HIHH 1142
Cdd:cd06637   94 GSVTDLIKNTkgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRTVgRRNT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVIQ-----GIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVdfSFPHEYFCGVSNAARDF 1217
Cdd:cd06637  171 FIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN--PAPRLKSKKWSKKFQSF 248
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1218 INVILQEDFRRRPTAATCLQHPWL--QPH 1244
Cdd:cd06637  249 IESCLVKNHSQRPSTEQLMKHPFIrdQPN 277
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
986-1241 1.07e-13

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: 72.47  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ---AAHEAALLQHLQHPQYITLHDTYESPTSYILI-LE 1061
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRErkaAEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIvMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHD--ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENL-LIDLRIpvprVKLIDLEDAVQISGHF 1138
Cdd:cd08223   81 FCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIfLTKSNI----IKVGDLGIARVLESSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHH-LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF-SFPHEYfcgvSNAARD 1216
Cdd:cd08223  157 DMATtLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQY----SPELGE 232
                        250       260
                 ....*....|....*....|....*
gi 68362740 1217 FINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd08223  233 LIKAMLHQDPEKRPSVKRILRQPYI 257
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
1003-1241 1.14e-13

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: 72.08  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1003 KCIHKATRKDVAVKFVSKKMKKKEQAAHeaalLQHLQHPQYITLHDTYeSPTSYILILELMDDGRLLDYLMNHDELMEEK 1082
Cdd:cd13976   11 RCVDIHTGEELVCKVVPVPECHAVLRAY----FRLPSHPNISGVHEVI-AGETKAYVFFERDHGDLHSYVRSRKRLREPE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1083 VAFYIRDIMEALQYLHNCRVAHLDIKpenllidLRIPV------PRVKLIDLEDAVQISGHFH-IHHLLGNPEFAAPEVI 1155
Cdd:cd13976   86 AARLFRQIASAVAHCHRNGIVLRDLK-------LRKFVfadeerTKLRLESLEDAVILEGEDDsLSDKHGCPAYVSPEIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1156 --QGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINVILQEDFRRRPTAA 1233
Cdd:cd13976  159 nsGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPE----TLSPRARCLIRSLLRREPSERLTAE 234

                 ....*...
gi 68362740 1234 TCLQHPWL 1241
Cdd:cd13976  235 DILLHPWL 242
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
990-1242 1.17e-13

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: 72.86  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVK--FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTY--ESPTsYILILELMDD 1065
Cdd:cd06620   10 LKDLGAGNGGSVSKVLHIPTGTIMAKKviHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFlnENNN-IIICMEYMDC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNC-RVAHLDIKPENLLIDLRipvPRVKLIDLedavQISGHFhIHHL- 1143
Cdd:cd06620   89 GSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSK---GQIKLCDF----GVSGEL-INSIa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 ---LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV---------CRV---------DFSF 1202
Cdd:cd06620  161 dtfVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGpmgildllqRIVneppprlpkDRIF 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1203 PHEyfcgvsnaARDFINVILQEDFRRRPTAAT-CLQHPWLQ 1242
Cdd:cd06620  241 PKD--------LRDFVDRCLLKDPRERPSPQLlLDHDPFIQ 273
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
1039-1190 1.24e-13

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: 73.40  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1039 QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRi 1118
Cdd:cd05590   54 NHPFLTQLYCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHE- 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1119 pvPRVKLIDLEDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE 1190
Cdd:cd05590  133 --GHCKLADFGMCKEgIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDD 203
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
987-1180 1.69e-13

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: 72.40  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK-FVSKKM--KKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKkFVESEDdpVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDgRLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDledavqisghFHIHH 1142
Cdd:cd07847   83 DH-TVLNELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQ---GQIKLCD----------FGFAR 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1143 LLGNPE-----------FAAPEVI-----QGIPVslgtDIWSIGVLTYVMLSGV 1180
Cdd:cd07847  149 ILTGPGddytdyvatrwYRAPELLvgdtqYGPPV----DVWAIGCVFAELLTGQ 198
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
987-1212 1.69e-13

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: 73.10  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd07872    8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApcTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGrLLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFHIH 1141
Cdd:cd07872   88 KD-LKQYMDDCGNIMSmHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADfgLARAKSVPTKTYSN 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1142 HLLgNPEFAAPEVIQGIP-VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd07872  164 EVV-TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISS 234
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
993-1203 1.86e-13

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: 73.11  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKF----VSKKMKKKEQAAHEAALLQHLQHPQYIT-LHDTYESPTSYILILELMDDGR 1067
Cdd:cd05615   18 LGKGSFGKVMLAERKGSDELYAIKIlkkdVVIQDDDVECTMVEKRVLALQDKPPFLTqLHSCFQTVDRLYFVMEYVNGGD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDL----EDAVQisgHFHIHHL 1143
Cdd:cd05615   98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSE---GHIKIADFgmckEHMVE---GVTTRTF 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP 1203
Cdd:cd05615  172 CGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP 231
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
791-865 2.59e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 66.20  E-value: 2.59e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740  791 VILQCKVCGRPKPTITWKGPDQNILDTDNSSATYTVSSCdsgeiTLKICNLMPQDSGIYTCIATNDHGTTSTSAT 865
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNG-----TLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
993-1190 2.93e-13

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: 72.33  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKK---------MKKKEQAAHEAAllQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGELFAIKALKKGdiiardeveSLMCEKRIFETV--NSARHPFLVNLFACFQTPEHVCFVMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGrllDYLMN-HDELMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF-HI 1140
Cdd:cd05589   85 AGG---DLMMHiHEDVFSEPRAvFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLCKEGMGFGdRT 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE 1190
Cdd:cd05589  159 STFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEE 208
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
986-1183 3.65e-13

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: 72.03  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE--QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07869    6 SYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTpfTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGrLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLID--LEDAVQISGHFHI 1140
Cdd:cd07869   86 HTD-LCQYMDKHpGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS---DTGELKLADfgLARAKSVPSHTYS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 68362740 1141 HHLLgNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd07869  162 NEVV-TLWYRPPDVLLGsTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
990-1241 4.09e-13

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: 71.21  E-value: 4.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL 1068
Cdd:cd06643   10 VGELGDGAFGKVYKAQNKETGILAAAKVIdTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 lDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIH-HLLG 1145
Cdd:cd06643   90 -DAVMLELErpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLD---GDIKLADFGVSAKNTRTLQRRdSFIG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1146 NPEFAAPEVI-----QGIPVSLGTDIWSIGVlTYVMLSGVSPFLDEskeetcINVCRVDFSFPHEYFCGVSNAAR----- 1215
Cdd:cd06643  166 TPYWMAPEVVmcetsKDRPYDYKADVWSLGV-TLIEMAQIEPPHHE------LNPMRVLLKIAKSEPPTLAQPSRwspef 238
                        250       260
                 ....*....|....*....|....*..
gi 68362740 1216 -DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06643  239 kDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
993-1203 4.91e-13

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: 71.57  E-value: 4.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKF----VSKKMKKKEQAAHEAALLQHLQHPQYIT-LHDTYESPTSYILILELMDDGR 1067
Cdd:cd05616    8 LGKGSFGKVMLAERKGTDELYAVKIlkkdVVIQDDDVECTMVEKRVLALSGKPPFLTqLHSCFQTMDRLYFVMEYVNGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID-------LEDAVQISGhfhi 1140
Cdd:cd05616   88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSE---GHIKIADfgmckenIWDGVTTKT---- 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1141 hhLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP 1203
Cdd:cd05616  161 --FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYP 221
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
973-1242 5.19e-13

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: 71.62  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  973 DGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHD 1048
Cdd:cd06635   13 DIAELFFKEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqdiIKEVKFLQRIKHPNSIEYKG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1049 TYESPTSYILILELMDdGRLLDYLMNHDELMEE-KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLID 1127
Cdd:cd06635   93 CYLREHTAWLVMEYCL-GSASDLLEVHKKPLQEiEIAAITHGALQGLAYLHSHNMIHRDIKAGNILL---TEPGQVKLAD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1128 LEDAVQISGhfhIHHLLGNPEFAAPEVIQGIPVSL---GTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDfsFPH 1204
Cdd:cd06635  169 FGSASIASP---ANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNE--SPT 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 68362740 1205 EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06635  244 LQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVL 281
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
987-1245 5.62e-13

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: 72.00  E-value: 5.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS---KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS------YI 1057
Cdd:cd07878   17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSrpfQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSienfneVY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMddGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLRIpvprvklIDLEDAVQ 1133
Cdd:cd07878   97 LVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVnedcELRI-------LDFGLARQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ----ISGHfhihhlLGNPEFAAPEV-IQGIPVSLGTDIWSIGVLTYVMLSGVSPF-----LDESKE----------ETCI 1193
Cdd:cd07878  168 addeMTGY------VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFpgndyIDQLKRimevvgtpspEVLK 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1194 NVC-----RVDFSFPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL-QPHN 1245
Cdd:cd07878  242 KISseharKYIQSLPHmpqqdlkKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFsQYHD 306
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
774-868 5.90e-13

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 65.59  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNIldTDNSSATYTVSscDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:cd05744    1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPV--RPDSAHKMLVR--ENGRHSLIIEPVTKRDAGIYTCIA 76
                         90
                 ....*....|....*
gi 68362740  854 TNDHGTTSTSATVKV 868
Cdd:cd05744   77 RNRAGENSFNAELVV 91
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
985-1244 5.94e-13

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: 71.24  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQHPQYITLHD--TYESPTSYILI 1059
Cdd:cd07845    7 TEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGipiSSLREITLLLNLRHPNIVELKEvvVGKHLDSIFLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LEL--MDDGRLLDYLMNhdELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDledavqisgh 1137
Cdd:cd07845   87 MEYceQDLASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIAD---------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLLGNPE-----------FAAPEVIQGIPV-SLGTDIWSIGVLTYVMLSGvSPFLDESKEETCIN-VCRV------ 1198
Cdd:cd07845  152 FGLARTYGLPAkpmtpkvvtlwYRAPELLLGCTTyTTAIDMWAVGCILAELLAH-KPLLPGKSEIEQLDlIIQLlgtpne 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1199 -------------DFSFPHE-Y------FCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd07845  231 siwpgfsdlplvgKFTLPKQpYnnlkhkFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEK 296
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
985-1219 6.83e-13

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: 71.66  E-value: 6.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP-----QYITLHDTYESPTSYILI 1059
Cdd:cd14227   15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNHTCLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDgRLLDYL-MNHDELMEEKvafYIRDIME----ALQYLHNCRVAHLDIKPEN-LLIDLRIPVPRVKLIDLEDAVQ 1133
Cdd:cd14227   95 FEMLEQ-NLYDFLkQNKFSPLPLK---YIRPILQqvatALMKLKSLGLIHADLKPENiMLVDPSRQPYRVKVIDFGSASH 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGHFhIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGvSPFLDESKEETCINVCRVDFSFPHEYFCGVSNA 1213
Cdd:cd14227  171 VSKAV-CSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLYPGASEYDQIRYISQTQGLPAEYLLSAGTK 248

                 ....*.
gi 68362740 1214 ARDFIN 1219
Cdd:cd14227  249 TTRFFN 254
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
985-1190 8.23e-13

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: 69.98  E-value: 8.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHLGYWLNKDK-VAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENLLID----LRIPVPRVKLIDLEDAVQIS--GH 1137
Cdd:cd05112   83 HGCLSDYLRTQRGLFSAETLLGMcLDVCEGMAYLEEASVIHRDLAARNCLVGenqvVKVSDFGMTRFVLDDQYTSStgTK 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1138 FHIhhllgnpEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEE 1190
Cdd:cd05112  163 FPV-------KWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSE 209
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
992-1183 8.46e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 70.46  E-value: 8.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVA---VKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS----YILILELMD 1064
Cdd:cd14030   32 EIGRGSFKTVYKGLDTETTVEVAwceLQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR--VAHLDIKPENLLIDLriPVPRVKLIDLEDAVQISGHFhIHH 1142
Cdd:cd14030  112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITG--PTGSVKIGDLGLATLKRASF-AKS 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1143 LLGNPEFAAPEVIQGiPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14030  189 VIGTPEFMAPEMYEE-KYDESVDVYAFGMCMLEMATSEYPY 228
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
987-1244 1.12e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 70.47  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--------AAHEAALLQHLQHPQYITLHDTYESPT-SYI 1057
Cdd:cd14041    8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdSFC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMdDGRLLDYLMNHDELMEEKVA-FYIRDIMEALQYLHNCR--VAHLDIKPENLLIDLRIPVPRVKLIDL------ 1128
Cdd:cd14041   88 TVLEYC-EGNDLDFYLKQHKLMSEKEArSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITDFglskim 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 --EDAVQISGHFHIHHLLGNPEFAAPE--VIQGIP--VSLGTDIWSIGVLTYVMLSGVSPF------LDESKEETCINVC 1196
Cdd:cd14041  167 ddDSYNSVDGMELTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFghnqsqQDILQENTILKAT 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1197 RVDFSfPHEyfcGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd14041  247 EVQFP-PKP---VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPH 290
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
1035-1239 2.29e-12

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: 68.54  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1035 LQHLQHPQYITLHD-TYESPTS------YILiLELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDI 1107
Cdd:cd14012   52 LKKLRHPNLVSYLAfSIERRGRsdgwkvYLL-TEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1108 KPENLLIDLRIPVPRVKLID--LEDAVQISGHFHIHHLLGNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFl 1184
Cdd:cd14012  131 HAGNVLLDRDAGTGIVKLTDysLGKTLLDMCSRGSLDEFKQTYWLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGLDVL- 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1185 desKEETCINVCRVDFSFPHEYfcgvsnaaRDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd14012  210 ---EKYTSPNPVLVSLDLSASL--------QDFLSKCLSLDPKKRPTALELLPHE 253
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
983-1244 2.34e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 69.32  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQ--------AAHEAALLQHLQHPQYITLHDTYESPT 1054
Cdd:cd14040    4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 -SYILILELMdDGRLLDYLMNHDELMEEKVAFYI-RDIMEALQYLHNCR--VAHLDIKPENLLIDLRIPVPRVKLIDL-- 1128
Cdd:cd14040   84 dTFCTVLEYC-EGNDLDFYLKQHKLMSEKEARSIvMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFgl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 -----EDAVQISGHFHIHHLLGNPEFAAPE--VIQGIP--VSLGTDIWSIGVLTYVMLSGVSPF------LDESKEETCI 1193
Cdd:cd14040  163 skimdDDSYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTIL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1194 NVCRVDFSFPHEyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd14040  243 KATEVQFPVKPV----VSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPH 289
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1039-1190 2.60e-12

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: 69.44  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1039 QHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRi 1118
Cdd:cd05591   54 KHPFLTALHSCFQTKDRLFFVMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE- 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1119 pvPRVKLIDLEDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE 1190
Cdd:cd05591  133 --GHCKLADFGMCKEgILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDD 203
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
781-868 2.61e-12

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 63.57  E-value: 2.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  781 VDVTCLLGDTVILQCKVCGRPKPTITWKGPDQN-------ILDtDNSsatytvsscdsgeitLKICNLMPQDSGIYTCIA 853
Cdd:cd05725    5 QNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGElpkgryeILD-DHS---------------LKIRKVTAGDMGSYTCVA 68
                         90
                 ....*....|....*
gi 68362740  854 TNDHGTTSTSATVKV 868
Cdd:cd05725   69 ENMVGKIEASATLTV 83
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
987-1242 2.65e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 69.08  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:PLN00009    4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEgvpSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1064 DdgrlLDYLMNHDELME-----EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHF 1138
Cdd:PLN00009   84 D----LDLKKHMDSSPDfaknpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALKLADFGLARAFGIPVRT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1139 HIHHLLgNPEFAAPEVIQGI-PVSLGTDIWSIGVLTYVMLSGVSPFLDESK---------------EETCINVCRV-DF- 1200
Cdd:PLN00009  160 FTHEVV-TLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEidelfkifrilgtpnEETWPGVTSLpDYk 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 68362740  1201 -SFPH-------EYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:PLN00009  239 sAFPKwppkdlaTVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
779-868 2.83e-12

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 63.75  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  779 PLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDtdnsSATYTVSSCDSGEITLKICNLMPQDSGIYTCIATNDHG 858
Cdd:cd20973    3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVE----SRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLG 78
                         90
                 ....*....|
gi 68362740  859 TTSTSATVKV 868
Cdd:cd20973   79 EATCSAELTV 88
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
993-1183 2.90e-12

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: 68.69  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALlqhlQHPQYITLHDTY-ESPTSYILiLELMDDGRLLDY 1071
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGL----TSPRVVPLYGAVrEGPWVNIF-MDLKEGGSLGQL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRipvpRVKLID------LEDAVQISGHFHIHHL 1143
Cdd:cd13991   89 IKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLssDGS----DAFLCDfghaecLDPDGLGKSLFTGDYI 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd13991  165 PGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
981-1189 3.03e-12

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: 69.66  E-value: 3.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALL----QHLQHPQY--ITLHDTYESPT 1054
Cdd:cd14226    9 EKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLelmnKHDTENKYyiVRLKRHFMFRN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 SYILILELMdDGRLLDYLMNHDE-----LMEEKVAFyirDIMEALQYLH--NCRVAHLDIKPENLLidLRIP-VPRVKLI 1126
Cdd:cd14226   89 HLCLVFELL-SYNLYDLLRNTNFrgvslNLTRKFAQ---QLCTALLFLStpELSIIHCDLKPENIL--LCNPkRSAIKII 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1127 DLEDAVQISGhfHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGvSPFLDESKE 1189
Cdd:cd14226  163 DFGSSCQLGQ--RIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLFSGANE 222
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
987-1238 3.60e-12

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: 68.48  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQHPQYITLHD------TYESPTSYILi 1059
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILcHSKEDVKEAMREIENYRLFNHPNILRLLDsqivkeAGGKKEVYLL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYL----MNHDELMEEKVAFYIRDIMEALQYLHNCR---VAHLDIKPENLLIDL-RIPVprvkLIDLEDA 1131
Cdd:cd13986   81 LPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEdDEPI----LMDLGSM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 VQ----ISGhfhIHHLLGNPEFA---------APE---VIQGIPVSLGTDIWSIGVLTYVMLSGVSPF-LDESKEETC-I 1193
Cdd:cd13986  157 NParieIEG---RREALALQDWAaehctmpyrAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPFeRIFQKGDSLaL 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 68362740 1194 NVCRVDFSFPHEyfCGVSNAARDFINVILQEDFRRRPTAATCLQH 1238
Cdd:cd13986  234 AVLSGNYSFPDN--SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
787-963 3.69e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.80  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  787 LGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCI--ATNDHGTTSTSA 864
Cdd:COG3401  143 LGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRvaATDTGGESAPSN 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  865 TVKVQGVPAAPNRPI---AQERSCTSVILRWLPPSSTGnctISGYTVEYREEGSQIWQQsVASTLDTYLVIEDLSPGCPY 941
Cdd:COG3401  223 EVSVTTPTTPPSAPTgltATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTK-VATVTTTSYTDTGLTNGTTY 298
                        170       180
                 ....*....|....*....|..
gi 68362740  942 QFRVSASNPWGIslPSEPSEFV 963
Cdd:COG3401  299 YYRVTAVDAAGN--ESAPSNVV 318
fn3 pfam00041
Fibronectin type III domain;
874-957 4.02e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 4.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    874 APNRPIAQERSCTSVILRWLPPSsTGNCTISGYTVEYREEGSQ-IWQ-QSVASTLDTYlVIEDLSPGCPYQFRVSASNPW 951
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGePWNeITVPGTTTSV-TLTGLKPGTEYEVRVQAVNGG 79

                   ....*.
gi 68362740    952 GISLPS 957
Cdd:pfam00041   80 GEGPPS 85
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
992-1242 4.50e-12

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 68.86  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFS--IVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDG 1066
Cdd:cd08216    5 EIGKCFKGggVVHLAKHKPTNTLVAVKKINLESDSKEdlkFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISG-------- 1136
Cdd:cd08216   85 SCRDLLKTHfpEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILIS---GDGKVVLSGLRYAYSMVKhgkrqrvv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHLLGNPEFAAPEVI-QGIpvsLG----TDIWSIGVLTYVMLSGVSPFLD-------------------------- 1185
Cdd:cd08216  162 HDFPKSSEKNLPWLSPEVLqQNL---LGynekSDIYSVGITACELANGVVPFSDmpatqmllekvrgttpqlldcstypl 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1186 ----ESKEETCINVCRVDFSFPHEYFCGV-SNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd08216  239 eedsMSQSEDSSTEHPNNRDTRDIPYQRTfSEAFHQFVELCLQRDPELRPSASQLLAHSFFK 300
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
1010-1242 4.97e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 70.05  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1010 RKDVAVKFVskKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRL----LDYLMNHDELMEEK 1082
Cdd:PTZ00267   93 KEKVVAKFV--MLNDERQAAYarsELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLnkqiKQRLKEHLPFQEYE 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1083 VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLEDAVQISGHFHI---HHLLGNPEFAAPEVIQGIP 1159
Cdd:PTZ00267  171 VGLLFYQIVLALDEVHSRKMMHRDLKSANIFL---MPTGIIKLGDFGFSKQYSDSVSLdvaSSFCGTPYYLAPELWERKR 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1160 VSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS-FPheyfCGVSNAARDFINVILQEDFRRRPTAATCLQH 1238
Cdd:PTZ00267  248 YSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFP----CPVSSGMKALLDPLLSKNPALRPTTQQLLHT 323

                  ....
gi 68362740  1239 PWLQ 1242
Cdd:PTZ00267  324 EFLK 327
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
987-1179 6.19e-12

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 68.40  E-value: 6.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIH-KATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQH--PQ----YITLHDTYESPTSYILI 1059
Cdd:cd14135    2 YRVYGYLGKGVFSNVVRARDlARGNQEVAIKIIRNNELMHKAGLKELEILKKLNDadPDdkkhCIRLLRHFEHKNHLCLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDdgrlldylMNHDELMEE----------KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLE 1129
Cdd:cd14135   82 FESLS--------MNLREVLKKygknvglnikAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNT--LKLCDFG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740 1130 DAVQISGHfHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSG 1179
Cdd:cd14135  152 SASDIGEN-EITPYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTG 200
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
987-1241 6.24e-12

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: 67.14  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPkerEESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELM--EEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlripvpRVKLIDLedavqisGHFHIH 1141
Cdd:cd08218   82 DGGDLYKRINAQRGVLfpEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT------KDGIIKL-------GDFGIA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1142 HLL-----------GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDF-SFPHEYfcg 1209
Cdd:cd08218  149 RVLnstvelartciGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRY--- 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68362740 1210 vSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd08218  226 -SYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
980-1241 6.44e-12

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: 67.76  E-value: 6.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  980 KENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK-EQAAHEAALLQHLQHPQYITLHDTYESPTSYIL 1058
Cdd:cd06645    6 RRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDfAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1059 ILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLEDAVQISGHF 1138
Cdd:cd06645   86 CMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILL---TDNGHVKLADFGVSAQITATI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHH-LLGNPEFAAPEViQGIPVSLG----TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPH-EYFCGVSN 1212
Cdd:cd06645  163 AKRKsFIGTPYWMAPEV-AAVERKGGynqlCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKlKDKMKWSN 241
                        250       260
                 ....*....|....*....|....*....
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd06645  242 SFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
988-1191 6.79e-12

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: 67.09  E-value: 6.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  988 TELNEIGRGRFSIVKKCIHKATRkDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05059    7 TFLKELGSGQFGVVHLGKWRGKI-DVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprvKLID-------LEDAVQISG--H 1137
Cdd:cd05059   86 LLNYLRERRGKFQtEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVV---KVSDfglaryvLDDEYTSSVgtK 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1138 FHIhhllgnpEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEET 1191
Cdd:cd05059  163 FPV-------KWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEV 210
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
1042-1231 7.33e-12

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 67.31  E-value: 7.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1042 QYITLHDTYESPTSY-ILIL-ELMDDGRLLDyLMN---HDELMEEKVAFYIRDIMEALQYLHNCR--VAHLDIKPENLLI 1114
Cdd:cd14037   65 GYIDSSANRSGNGVYeVLLLmEYCKGGGVID-LMNqrlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLI 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1115 DLR------------IPVPRVKLIDLEDAVQ--ISGHfhihhllGNPEFAAPEVI---QGIPVSLGTDIWSIGVLTYVML 1177
Cdd:cd14037  144 SDSgnyklcdfgsatTKILPPQTKQGVTYVEedIKKY-------TTLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLC 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1178 SGVSPFlDESKEetcINVCRVDFSFP--HEYfcgvSNAARDFINVILQEDFRRRPT 1231
Cdd:cd14037  217 FYTTPF-EESGQ---LAILNGNFTFPdnSRY----SKRLHKLIRYMLEEDPEKRPN 264
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
992-1183 7.96e-12

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 67.02  E-value: 7.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKDVA---VKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS----YILILELMD 1064
Cdd:cd14032    8 ELGRGSFKTVYKGLDTETWVEVAwceLQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCR--VAHLDIKPENLLIDLriPVPRVKLIDLEDAVQISGHFhIHH 1142
Cdd:cd14032   88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITG--PTGSVKIGDLGLATLKRASF-AKS 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1143 LLGNPEFAAPEVIQGiPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14032  165 VIGTPEFMAPEMYEE-HYDESVDVYAFGMCMLEMATSEYPY 204
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
1064-1241 8.17e-12

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: 66.61  E-value: 8.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1064 DDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGH---FHI 1140
Cdd:cd14023   67 DFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDE-ERTQLRLESLEDTHIMKGEddaLSD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHllGNPEFAAPEVIQ--GIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEyfcgVSNAARDFI 1218
Cdd:cd14023  146 KH--GCPAYVSPEILNttGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDH----VSPKARCLI 219
                        170       180
                 ....*....|....*....|...
gi 68362740 1219 NVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14023  220 RSLLRREPSERLTAPEILLHPWF 242
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
990-1265 8.43e-12

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: 67.21  E-value: 8.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd06619    6 QEILGHGNGGTVYKAYHLLTRRILAVKVIplDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYlmnhdELMEEKVAFYIR-DIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFHIHHLlGN 1146
Cdd:cd06619   86 LDVY-----RKIPEHVLGRIAvAVVKGLTYLWSLKILHRDVKPSNMLVNTR---GQVKLCDFGVSTQLVNSIAKTYV-GT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETC-----INVCRVDFSFPHEYFCGVSNAARDFINVI 1221
Cdd:cd06619  157 NAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSlmplqLLQCIVDEDPPVLPVGQFSEKFVHFITQC 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 68362740 1222 LQEDFRRRPTAATCLQHPWL-QPHNGSYSKIPLDTSRlaCFIERR 1265
Cdd:cd06619  237 MRKQPKERPAPENLMDHPFIvQYNDGNAEVVSMWVCR--ALEERR 279
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
993-1203 8.44e-12

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: 67.80  E-value: 8.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKF----VSKKMKKKEQAAHEAALLQHLQHPQYIT-LHDTYESPTSYILILELMDDGR 1067
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELYAIKIlkkdVIIQDDDVECTMVEKRVLALSGKPPFLTqLHSCFQTMDRLYFVMEYVNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ-ISGHFHIHHLLGN 1146
Cdd:cd05587   84 LMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAE---GHIKIADFGMCKEgIFGGKTTRTFCGT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1147 PEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFP 1203
Cdd:cd05587  161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP 217
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
773-868 9.33e-12

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 9.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  773 APEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWkgpdqnILDTDNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCI 852
Cdd:cd20976    1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITW------IRNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCL 74
                         90
                 ....*....|....*.
gi 68362740  853 ATNDHGTTSTSATVKV 868
Cdd:cd20976   75 AKNAAGQVSCSAWVTV 90
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
774-869 9.85e-12

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 62.44  E-value: 9.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNIlDTDNSSATYTVSScDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:cd20951    1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPI-DPSSIPGKYKIES-EYGVHVLHIRRVTVEDSAVYSAVA 78
                         90
                 ....*....|....*.
gi 68362740  854 TNDHGTTSTSATVKVQ 869
Cdd:cd20951   79 KNIHGEASSSASVVVE 94
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
981-1238 1.18e-11

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: 66.75  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSkkmKKKEQAAHEAALLQHLQHPQYITLHDTYESP------- 1053
Cdd:cd14047    2 ERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK---LNNEKAEREVKALAKLDHPNIVRYNGCWDGFdydpets 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 --------TSYILI-LELMDDGRLLDYL--MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPR 1122
Cdd:cd14047   79 ssnssrskTKCLFIqMEFCEKGTLESWIekRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFL---VDTGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1123 VKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETciNVCRVDFSf 1202
Cdd:cd14047  156 VKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWT--DLRNGILP- 232
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 68362740 1203 phEYFCGVSNAARDFINVILQEDFRRRPTAATCLQH 1238
Cdd:cd14047  233 --DIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
983-1241 2.29e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 66.97  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQhlqhpqyiTLHDTYESPTSYILILEL 1062
Cdd:cd14218    8 FNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLK--------CVRDSDPSDPKRETIVQL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGR-------------------LLDYLM--NHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLIDLR--- 1117
Cdd:cd14218   80 IDDFKisgvngvhvcmvlevlghqLLKWIIksNYQGLPLPCVKSILRQVLQGLDYLHTkCKIIHTDIKPENILMCVDegy 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1118 ---------------IPVP-------------------------RVKLIDLEDAVQIsgHFHIHHLLGNPEFAAPEVIQG 1157
Cdd:cd14218  160 vrrlaaeatiwqqagAPPPsgssvsfgasdflvnplepqnadkiRVKIADLGNACWV--HKHFTEDIQTRQYRALEVLIG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1158 IPVSLGTDIWSIGVLTYVMLSGVSPF-----LDESKEETCI-NVCRVDFSFP----------HEYFC------------- 1208
Cdd:cd14218  238 AEYGTPADIWSTACMAFELATGDYLFephsgEDYTRDEDHIaHIVELLGDIPphfalsgrysREYFNrrgelrhiknlkh 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1209 -------------GVSNAAR--DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14218  318 wglyevlvekyewPLEQAAQftDFLLPMMEFLPEKRATAAQCLQHPWL 365
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
993-1172 3.03e-11

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: 65.20  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKfvsKKMKKKEQAA--HEAALLQHLQHPQY-----ITLHDTYESPtsyilILELMDD 1065
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMK---ELKRFDEQRSflKEVKLMRRLSHPNIlrfigVCVKDNKLNF-----ITEYVNG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENLLI--------------DLRIPVPRVKLIDLED 1130
Cdd:cd14065   73 GTLEELLKSMDEQLPWSQRVSLaKDIASGMAYLHSKNIIHRDLNSKNCLVreanrgrnavvadfGLAREMPDEKTKKPDR 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1131 AVQISghfhihhLLGNPEFAAPEVIQGIPVSLGTDIWSIGVL 1172
Cdd:cd14065  153 KKRLT-------VVGSPYWMAPEMLRGESYDEKVDVFSFGIV 187
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
987-1170 3.16e-11

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: 66.32  E-value: 3.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP-----QYITLHDTYESPTSYILILE 1061
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGrLLDYLMNHDelMEEKVAFYIRDIME----ALQYLHNCRVAHLDIKPEN-LLID-LRIPVpRVKLIDLEDAVQIS 1135
Cdd:cd14211   81 MLEQN-LYDFLKQNK--FSPLPLKYIRPILQqvltALLKLKSLGLIHADLKPENiMLVDpVRQPY-RVKVIDFGSASHVS 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 68362740 1136 GHFHIHHLLGNpEFAAPEVIQGIPVSLGTDIWSIG 1170
Cdd:cd14211  157 KAVCSTYLQSR-YYRAPEIILGLPFCEAIDMWSLG 190
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
1066-1241 3.70e-11

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: 64.67  E-value: 3.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRiPVPRVKLIDLEDAVQISGH---FHIHH 1142
Cdd:cd14022   69 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDE-ERTRVKLESLEDAYILRGHddsLSDKH 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 llGNPEFAAPEVIQ--GIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINV 1220
Cdd:cd14022  148 --GCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE----TLSPKAKCLIRS 221
                        170       180
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14022  222 ILRREPSERLTSQEILDHPWF 242
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
776-868 4.01e-11

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 60.59  E-value: 4.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  776 FLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKgPDQNILDTDNSSATytvsSCDSGeiTLKICNLMPQDSGIYTCIATN 855
Cdd:cd20952    2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWL-KDGVPLLGKDERIT----TLENG--SLQIKGAEKSDTGEYTCVALN 74
                         90
                 ....*....|...
gi 68362740  856 DHGTTSTSATVKV 868
Cdd:cd20952   75 LSGEATWSAVLDV 87
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
973-1242 4.09e-11

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: 65.81  E-value: 4.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  973 DGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQA----AHEAALLQHLQHPQYITLHD 1048
Cdd:cd06634    3 EVAELFFKDDPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwqdiIKEVKFLQKLRHPNTIEYRG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1049 TYESPTSYILILELMDdGRLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLID 1127
Cdd:cd06634   83 CYLREHTAWLVMEYCL-GSASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLT---EPGLVKLGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1128 LEDAVQISGhfhIHHLLGNPEFAAPEVIQGIPVSL---GTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCR-----VD 1199
Cdd:cd06634  159 FGSASIMAP---ANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQnespaLQ 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1200 FSFPHEYFcgvsnaaRDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06634  236 SGHWSEYF-------RNFVDSCLQKIPQDRPTSDVLLKHRFLL 271
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
988-1242 4.37e-11

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: 65.46  E-value: 4.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  988 TELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAheaaLLQHLQH-------PQYITLHDTYESPTSYILIL 1060
Cdd:cd06616    9 KDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKR----LLMDLDVvmrssdcPYIVKFYGALFREGDCWICM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGrlLD------YLMNHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLIDLRipvPRVKLIDLedavQ 1133
Cdd:cd06616   85 ELMDIS--LDkfykyvYEVLDSVIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILLDRN---GNIKLCDF----G 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGH----FHIHHLLGNPEFAAPEVIQGIPVSLG----TDIWSIGVLTYVMLSGVSPF--LDESKEETCINVCRVDFSFP 1203
Cdd:cd06616  156 ISGQlvdsIAKTRDAGCRPYMAPERIDPSASRDGydvrSDVWSLGITLYEVATGKFPYpkWNSVFDQLTQVVKGDPPILS 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 68362740 1204 HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06616  236 NSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIK 274
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
984-1199 4.60e-11

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: 65.85  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd06650    4 DDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIhlEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYL-HNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFhI 1140
Cdd:cd06650   84 HMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLIDSM-A 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF-LDESKEETCINVCRVD 1199
Cdd:cd06650  160 NSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpPPDAKELELMFGCQVE 219
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
788-868 4.60e-11

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 60.17  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  788 GDTVILQCKVCGRPKPTITWKGPDQNIldTDNSSATYTvsscDSGeiTLKICNLMPQDSGIYTCIATNDHGTTSTSATVK 867
Cdd:cd04969   17 GGDVIIECKPKASPKPTISWSKGTELL--TNSSRICIL----PDG--SLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLS 88

                 .
gi 68362740  868 V 868
Cdd:cd04969   89 V 89
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
1031-1242 4.86e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 66.05  E-value: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1031 EAALLQHLQHPQYITLHDTYES-PTSYILILELMDDgrLLDYLMNHDELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIK 1108
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSgAITCMVLPHYSSD--LYTYLTKRSRPLPIDQALIIeKQILEGLRYLHAQRIIHRDVK 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1109 PENLLIDlriPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESK 1188
Cdd:PHA03209  185 TENIFIN---DVDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPP 261
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740  1189 eetcinvcrvdfSFPHEYFCGVSNAARDFINV--ILQEDFRRRPTA---------ATCLQHPWLQ 1242
Cdd:PHA03209  262 ------------STPEEYVKSCHSHLLKIISTlkVHPEEFPRDPGSrlvrgfieyASLERQPYTR 314
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
224-397 5.47e-11

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 67.61  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  224 EQKAKALRGRMFVLNELVQTEKDYVKDLGIVVEGFMKRIEE-KGVPEDMRGK-DKIVFGNIHQIYDWHKDFF--LAELEK 299
Cdd:COG5422  476 ESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEEsNIIPENARRNfIKHVFANINEIYAVNSKLLkaLTNRQC 555
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  300 CIQEQDRLAQLFIKHERKLHIYVWYCQNKPRSEYI----------VAEYDAYFEEVKQeiNQRLTLSDFLIKPIQRITKY 369
Cdd:COG5422  556 LSPIVNGIADIFLDYVPKFEPFIKYGASQPYAKYEfereksvnpnFARFDHEVERLDE--SRKLELDGYLTKPTTRLARY 633
                        170       180
                 ....*....|....*....|....*...
gi 68362740  370 QLLLKDFLRYSEKAGLECSDIEKAVELM 397
Cdd:COG5422  634 PLLLEEVLKFTDPDNPDTEDIPKVIDML 661
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
987-1193 5.83e-11

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: 65.49  E-value: 5.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP----QYITLH--DTYESPTSYILIL 1060
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILDALRRKdrdnSHNVIHmkEYFYFRNHLCITF 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDdgrlldylMNHDELMeEKVAF------YIR----DIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLED 1130
Cdd:cd14225  125 ELLG--------MNLYELI-KKNNFqgfslsLIRrfaiSLLQCLRLLYRERIIHCDLKPENILLRQRGQS-SIKVIDFGS 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1131 AVQIsgHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE--TCI 1193
Cdd:cd14225  195 SCYE--HQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEqlACI 257
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
987-1179 6.62e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 65.43  E-value: 6.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS---KKMKKKEQAAHEAALLQHLQHPQYITL------HDTYESPTSYI 1057
Cdd:cd07876   23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSrpfQNQTHAKRAYRELVLLKCVNHKNIISLlnvftpQKSLEEFQDVY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDdGRLLDYLmnHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPvprVKLIDLEDAVQISGH 1137
Cdd:cd07876  103 LVMELMD-ANLCQVI--HMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT---LKILDFGLARTACTN 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSG 1179
Cdd:cd07876  177 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKG 218
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
983-1241 7.25e-11

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 65.44  E-value: 7.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP--------QYITLHDTYE--- 1051
Cdd:cd14216    8 FNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSdpndpnreMVVQLLDDFKisg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1052 -SPTSYILILELMDDgRLLDYLM--NHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLIDL------RIPVP 1121
Cdd:cd14216   88 vNGTHICMVFEVLGH-HLLKWIIksNYQGLPLPCVKKIIRQVLQGLDYLHTkCRIIHTDIKPENILLSVneqyirRLAAE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1122 ---------------------RVKLIDLEDAVQISGHFhiHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGV 1180
Cdd:cd14216  167 atewqrnflvnplepknaeklKVKIADLGNACWVHKHF--TEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGD 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1181 SPFLDESKEETC------------------------------------------------INVCRVDFSFPHEYFCGVSn 1212
Cdd:cd14216  245 YLFEPHSGEDYSrdedhialiiellgkvprklivagkyskefftkkgdlkhitklkpwglFEVLVEKYEWSQEEAAGFT- 323
                        330       340
                 ....*....|....*....|....*....
gi 68362740 1213 aarDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14216  324 ---DFLLPMLELIPEKRATAAECLRHPWL 349
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
993-1239 7.41e-11

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: 64.37  E-value: 7.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHK-ATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQ---HPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd14052    8 IGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAkdrLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELCEN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRL---LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLRI---------PVPRvkLIDLE 1129
Cdd:cd14052   88 GSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLItfegTLKIgdfgmatvwPLIR--GIERE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1130 davqisghfhihhllGNPEFAAPEVIQGIPVSLGTDIWSIGVL-----TYVML--SGVSPFLDESKEETciNVCRVDFSF 1202
Cdd:cd14052  166 ---------------GDREYIAPEILSEHMYDKPADIFSLGLIlleaaANVVLpdNGDAWQKLRSGDLS--DAPRLSSTD 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740 1203 PHEYFCGVSNAARDFIN-VILQEDF------------RRRPTAATCLQHP 1239
Cdd:cd14052  229 LHSASSPSSNPPPDPPNmPILSGSLdrvvrwmlspepDRRPTADDVLATP 278
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
983-1236 1.42e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 65.91  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   983 FDSAYTELNE------IGRGRFSIVKKCIHKATRKDV---AVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP 1053
Cdd:PTZ00266    5 YDDGESRLNEyevikkIGNGRFGEVFLVKHKRTQEFFcwkAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1054 TS---YILiLELMDDGRLLD-----YLMnHDELMEEKVAFYIRDIMEALQYLHNC-------RVAHLDIKPENLLIDLRI 1118
Cdd:PTZ00266   85 ANqklYIL-MEFCDAGDLSRniqkcYKM-FGKIEEHAIVDITRQLLHALAYCHNLkdgpngeRVLHRDLKPQNIFLSTGI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1119 ----------------PVPRVKLIDLEDAVQISGHfhIHHLLGNPEFAAPEVIQGIPVSLG--TDIWSIGVLTYVMLSGV 1180
Cdd:PTZ00266  163 rhigkitaqannlngrPIAKIGDFGLSKNIGIESM--AHSCVGTPYYWSPELLLHETKSYDdkSDMWALGCIIYELCSGK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740  1181 SPFLDESKEETCINVCRVDFSFPHEyfcGVSNAARDFINVILQEDFRRRPTAATCL 1236
Cdd:PTZ00266  241 TPFHKANNFSQLISELKRGPDLPIK---GKSKELNILIKNLLNLSAKERPSALQCL 293
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
774-869 1.77e-10

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 58.49  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKgpdqNILDTDNSSATYTVSSCdsgeiTLKICNLMPQDSGIYTCIA 853
Cdd:cd05851    2 ADINVKFKDTYALKGQNVTLECFALGNPVPVIRWR----KILEPMPATAEISMSGA-----VLKIFNIQPEDEGTYECEA 72
                         90
                 ....*....|....*.
gi 68362740  854 TNDHGTTSTSATVKVQ 869
Cdd:cd05851   73 ENIKGKDKHQARVYVQ 88
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
993-1128 2.53e-10

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: 59.76  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFV-SKKMKKKEQAAHEAALLQ-----HLQHPQYItlhDTYESPTSYILILELMDDG 1066
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGdDVNNEEGEDLESEMDILRrlkglELNIPKVL---VTEDVDGPNILLMELVKGG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1067 RLLDYLMNhDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDL 1128
Cdd:cd13968   78 TLIAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS---EDGNVKLIDF 135
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
766-868 2.55e-10

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 58.34  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  766 PNFIQEVAPEFLVPlvdvtcllGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSATYTVSScdSGEIT--LKICNLMP 843
Cdd:cd20956    2 PVLLETFSEQTLQP--------GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTS--DGDVVsyVNISSVRV 71
                         90       100
                 ....*....|....*....|....*
gi 68362740  844 QDSGIYTCIATNDHGTTSTSATVKV 868
Cdd:cd20956   72 EDGGEYTCTATNDVGSVSHSARINV 96
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
987-1241 2.71e-10

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: 63.06  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALL---QHLQHPQYITLHDTYES-----PTS 1055
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGlplSTVREVALLkrlEAFDHPNIVRLMDVCATsrtdrETK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 YILILELMDDGrLLDYL--MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQ 1133
Cdd:cd07863   82 VTLVFEHVDQD-LRTYLdkVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVKLADFGLARI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEEtciNVCRV--------------D 1199
Cdd:cd07863  158 YSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEAD---QLGKIfdliglppeddwprD 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1200 FSFPHEYFC------------GVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07863  235 VTLPRGAFSprgprpvqsvvpEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
989-1183 2.78e-10

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 62.44  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNE-IGRGRFSIVKKCI---HKATRKDVAVKF--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYIlILEL 1062
Cdd:cd05056    9 TLGRcIGEGQFGDVYQGVymsPENEKIAVAVKTckNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPVWI-VMEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLidlrIPVPR-VKLIDLEDAVQISGHFHI 1140
Cdd:cd05056   88 APLGELRSYLqVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL----VSSPDcVKLGDFGLSRYMEDESYY 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 68362740 1141 HHLLGN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPF 1183
Cdd:cd05056  164 KASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPF 209
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
985-1197 2.90e-10

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: 62.57  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05114    4 SELTFMKELGSGLFGVVRLGKWRAQYK-VAIKAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIPVPRVK-------LIDLEDAVQISG 1136
Cdd:cd05114   83 NGCLLNYLrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVN-DTGVVKVSdfgmtryVLDDQYTSSSGA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1137 HFHIhhllgnpEFAAPEVIQGIPVSLGTDIWSIGVLTY-VMLSGVSPFLDESKEETCINVCR 1197
Cdd:cd05114  162 KFPV-------KWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSR 216
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
986-1198 3.82e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 63.90  E-value: 3.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVskkMKKKEQAAHEAALLQHLQHPQYITLHDTY--------ESPTSYI 1057
Cdd:PTZ00036   67 SYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV---LQDPQYKNRELLIMKNLNHINIIFLKDYYytecfkknEKNIFLN 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1058 LILELMDD---GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQI 1134
Cdd:PTZ00036  144 VVMEFIPQtvhKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHT--LKLCDFGSAKNL 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740  1135 SGHFHIHHLLGNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV 1198
Cdd:PTZ00036  222 LAGQRSVSYICSRFYRAPELMLGaTNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQV 286
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
988-1195 4.33e-10

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: 61.82  E-value: 4.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  988 TELNEIGRGRFSIVKKCIHKAtRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05113    7 TFLKELGTGQFGVVKYGKWRG-QYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVK-------LIDLEDAVQISGHFH 1139
Cdd:cd05113   86 LLNYLREMRKRFQtQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVV-KVSdfglsryVLDDEYTSSVGSKFP 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1140 IhhllgnpEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEETCINV 1195
Cdd:cd05113  165 V-------RWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHV 214
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
984-1244 4.58e-10

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 62.77  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTS----- 1055
Cdd:cd07858    4 DTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRtlrEIKLLRHLDHENVIAIKDIMPPPHReafnd 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 -YIlILELMDDGrLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----DLripvprvKLID--L 1128
Cdd:cd07858   84 vYI-VYELMDTD-LHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLnancDL-------KICDfgL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1129 EDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGV--------------------LTYVMLSGVSP------ 1182
Cdd:cd07858  155 ARTTSEKGDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCifaellgrkplfpgkdyvhqLKLITELLGSPseedlg 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1183 FLDESKEETCI----NVCRVDFS--FPHeyfcgVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd07858  235 FIRNEKARRYIrslpYTPRQSFArlFPH-----ANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASL 297
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
991-1183 4.71e-10

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: 61.60  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVKKCIH---KATRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPtSYILILELMDD 1065
Cdd:cd05060    1 KELGHGNFGSVRKGVYlmkSGKEVEVAVKTLKQEHEKAGKKEflREASVMAQLDHPCIVRLIGVCKGE-PLMLVMELAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFHIHHL 1143
Cdd:cd05060   80 GPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNR---HQAKISDfgMSRALGAGSDYYRATT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1144 LGN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPF 1183
Cdd:cd05060  157 AGRwPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPY 199
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
996-1237 5.31e-10

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: 62.14  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  996 GRFSIVKKC-IHKATRKDVAVKFvskkmkkkeqaaHEAALLQHLQHPQYITLHDTYESPTSYILILEL-MDDGRLLDYLM 1073
Cdd:cd14049   31 GQYYAIKKIlIKKVTKRDCMKVL------------REVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMqLCELSLWDWIV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1074 --------------NHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI----------DLRIPVPRVkLIDLE 1129
Cdd:cd14049   99 ernkrpceeefksaPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLhgsdihvrigDFGLACPDI-LQDGN 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1130 DAVQISGHFHIHHL--LGNPEFAAPEVIQGIPVSLGTDIWSIGVltyVMLSGVSPFLDESKEETCINVCRvDFSFPHEyF 1207
Cdd:cd14049  178 DSTTMSRLNGLTHTsgVGTCLYAAPEQLEGSHYDFKSDMYSIGV---ILLELFQPFGTEMERAEVLTQLR-NGQIPKS-L 252
                        250       260       270
                 ....*....|....*....|....*....|
gi 68362740 1208 CGVSNAARDFINVILQEDFRRRPTAATCLQ 1237
Cdd:cd14049  253 CKRWPVQAKYIKLLTSTEPSERPSASQLLE 282
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
993-1172 5.64e-10

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: 61.60  E-value: 5.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKAtrKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd05039   14 IGKGEFGDVMLGDYRG--QKVAVKCLKDDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVDYL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 -------MNHDELMEekvafYIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPVPRVKLIDLEDAVQISGHFHIhhl 1143
Cdd:cd05039   92 rsrgravITRKDQLG-----FALDVCEGMEYLESKKFVHRDLAARNVLVseDNVAKVSDFGLAKEASSNQDGGKLPI--- 163
                        170       180
                 ....*....|....*....|....*....
gi 68362740 1144 lgnpEFAAPEVIQGIPVSLGTDIWSIGVL 1172
Cdd:cd05039  164 ----KWTAPEALREKKFSTKSDVWSFGIL 188
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
984-1171 6.13e-10

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: 62.37  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  984 DSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd06649    4 DDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIhlEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYL-HNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHFhI 1140
Cdd:cd06649   84 HMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLIDSM-A 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 68362740 1141 HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGV 1171
Cdd:cd06649  160 NSFVGTRSYMSPERLQGTHYSVQSDIWSMGL 190
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
987-1242 6.13e-10

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: 62.07  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV--SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd06615    3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLIhlEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLH-NCRVAHLDIKPENLLIDLRipvPRVKLIDLedavQISGHFH---I 1140
Cdd:cd06615   83 GGSLDQVLKKAGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNILVNSR---GEIKLCDF----GVSGQLIdsmA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSP------------FLDESKE-ETCINVCRVDFSF----- 1202
Cdd:cd06615  156 NSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleamFGRPVSEgEAKESHRPVSGHPpdspr 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 68362740 1203 -------------------PHEYFcgvSNAARDFINVILQEDFRRRPTAATCLQHPWLQ 1242
Cdd:cd06615  236 pmaifelldyivnepppklPSGAF---SDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
849-977 6.30e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.48  E-value: 6.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  849 YTCIATNDHGTTST-SATVKVQGVPAAPNRPI---AQERSCTSVILRWLPPSSTGnctISGYTVEYREEGSQIWQQsVAS 924
Cdd:COG3401  300 YRVTAVDAAGNESApSNVVSVTTDLTPPAAPSgltATAVGSSSITLSWTASSDAD---VTGYNVYRSTSGGGTYTK-IAE 375
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740  925 TLD-TYLVIEDLSPGCPYQFRVSASNPWGISlpSEPSEFVRLPEYDAAADGATI 977
Cdd:COG3401  376 TVTtTSYTDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATTASAASGESLT 427
PH_Obscurin cd13239
Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; ...
413-524 6.54e-10

Obscurin pleckstrin homology (PH) domain; Obscurin (also called Obscurin-RhoGEF; Obscurin-myosin light chain kinase/Obscurin-MLCK) is a giant muscle protein that is concentrated at the peripheries of Z-disks and M-lines. It binds small ankyrin I, a component of the sarcoplasmic reticulum (SR) membrane. It is associated with the contractile apparatus through binding with titin and sarcomeric myosin. It plays important roles in the organization and assembly of the myofibril and the SR. Obscurin has been observed as alternatively-spliced isoforms. The major isoform in sleletal muscle, approximately 800 kDa in size, is composed of many adhesion modules and signaling domains. It harbors 49 Ig and 2 FNIII repeats at the N-terminues, a complex middle region with additional Ig domains, an IQ motif, and a conserved SH3 domain near RhoGEF and PH domains, and a non-modular C-terminus with phosphorylation motifs. The obscurin gene also encodes two kinase domains, which are not part of the 800 kDa form of the protein, but is part of smaller spliced products that present in heart muscle. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270059  Cd Length: 125  Bit Score: 58.32  E-value: 6.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  413 LQGFEGTLTAQGKLLQQDTFYVIELDAG--MQSRTKERRVFLFEQIVIFSELLRKGSL-TPGYMFKRSIKMNYLVLEENV 489
Cdd:cd13239    2 IENYPAPLQALGEPIRQGHFTVWEEAPEvkTSSRGHHRHVFLFKNCVVICKPKRDSRTdTVTYVFKNKMKLSDIDVKDTV 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 68362740  490 DNDPCKFALMN--RETSERVVLQAANADIQQAWVQDI 524
Cdd:cd13239   82 EGDDRSFGLWHehRGSVRKYTLQARSAIIKSSWLKDL 118
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
1035-1241 7.38e-10

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 61.01  E-value: 7.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1035 LQHLQHPQYITLH----DTYESPTSYILILELMDDGRLLDYL----MNHDELMEEKVAFYIRDIMEALQYLHNCRVAhld 1106
Cdd:cd13984   49 LIQLDHPNIVKFHrywtDVQEEKARVIFITEYMSSGSLKQFLkktkKNHKTMNEKSWKRWCTQILSALSYLHSCDPP--- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1107 IKPENLLIDlRIPVPRVKLIDLEDAVQISGHFHIHHLL---GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMlsgVSPF 1183
Cdd:cd13984  126 IIHGNLTCD-TIFIQHNGLIKIGSVAPDAIHNHVKTCReehRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEM---AALE 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1184 LDESKEETCIN---VCRVDFSFPheyfcgvSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd13984  202 IQSNGEKVSANeeaIIRAIFSLE-------DPLQKDFIRKCLSVAPQDRPSARDLLFHPVL 255
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
1027-1195 7.63e-10

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: 62.34  E-value: 7.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1027 QAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVA 1103
Cdd:cd05626   44 QVAHvkaERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1104 HLDIKPENLLIDLRipvPRVKLIDL----------------------EDAVQISGHFH---------------------- 1139
Cdd:cd05626  124 HRDIKPDNILIDLD---GHIKLTDFglctgfrwthnskyyqkgshirQDSMEPSDLWDdvsncrcgdrlktleqratkqh 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 ----IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV 1195
Cdd:cd05626  201 qrclAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKV 260
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
990-1231 7.70e-10

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: 61.21  E-value: 7.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd05072   12 VKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHD--ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRI-------PVPRVkLIDLEDAVQISGHFHI 1140
Cdd:cd05072   91 DFLKSDEggKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLmckiadfGLARV-IEDNEYTAREGAKFPI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1141 hhllgnpEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEETCINVCRvDFSFPHEYFCGVSnaARDFIN 1219
Cdd:cd05072  170 -------KWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQR-GYRMPRMENCPDE--LYDIMK 239
                        250
                 ....*....|..
gi 68362740 1220 VILQEDFRRRPT 1231
Cdd:cd05072  240 TCWKEKAEERPT 251
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
778-866 7.80e-10

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 56.82  E-value: 7.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    778 VPLVDVTCLLGDTVILQCKV-CGRPKPTITWKGPDQnildTDNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCIATND 856
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGG----TLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
                           90
                   ....*....|
gi 68362740    857 HGTTSTSATV 866
Cdd:pfam00047   77 GGSATLSTSL 86
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
787-869 8.73e-10

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 56.79  E-value: 8.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  787 LGDTVILQCKVCGRPKPTITWKgPDQNILDTDnssatyTVSSCDSGEITLKICNLMPQDSGIYTCIATNDHGttSTSATV 866
Cdd:cd05856   18 VGSSVRLKCVASGNPRPDITWL-KDNKPLTPP------EIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAG--EINATY 88

                 ...
gi 68362740  867 KVQ 869
Cdd:cd05856   89 KVD 91
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
990-1244 8.78e-10

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: 61.62  E-value: 8.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAA----HEAALLQHlQHPQYITLHDTYESPTSYILILELMdd 1065
Cdd:cd06618   20 LGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRilmdLDVVLKSH-DCPYIVKCYGYFITDSDVFICMELM-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYL---MNHDelMEEKVAFYIR-DIMEALQYL---HNcrVAHLDIKPENLLIDLRipvPRVKLIDLedavQISGHf 1138
Cdd:cd06618   97 STCLDKLlkrIQGP--IPEDILGKMTvSIVKALHYLkekHG--VIHRDVKPSNILLDES---GNVKLCDF----GISGR- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 hihhLL---------GNPEFAAPEVIQGIPVS---LGTDIWSIGVLTYVMLSGVSPFldeskeetciNVCRVDFSF---- 1202
Cdd:cd06618  165 ----LVdskaktrsaGCAAYMAPERIDPPDNPkydIRADVWSLGISLVELATGQFPY----------RNCKTEFEVltki 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1203 ---------PHEYFcgvSNAARDFINVILQEDFRRRPTAATCLQHPWLQPH 1244
Cdd:cd06618  231 lneeppslpPNEGF---SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRY 278
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
993-1183 1.17e-09

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: 60.39  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKAtrKDVAVKFVSK-----KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd14148    2 IGVGGFGKVYKGLWRG--EEVAVKAARQdpdedIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LldylmnHDELMEEKVAFYIR-----DIMEALQYLHN---CRVAHLDIKPENLLIdlripVPRVKLIDLEDAVQISGHFH 1139
Cdd:cd14148   80 L------NRALAGKKVPPHVLvnwavQIARGMNYLHNeaiVPIIHRDLKSSNILI-----LEPIENDDLSGKTLKITDFG 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1140 IHH---------LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14148  149 LARewhkttkmsAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
983-1239 1.18e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 60.81  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIH---------KATRKDVAVKfVSKKMKKKEQAAHeaALLQhlQHPQYITLHDTYESP 1053
Cdd:cd14138    3 YATEFHELEKIGSGEFGSVFKCVKrldgciyaiKRSKKPLAGS-VDEQNALREVYAH--AVLG--QHSHVVRYYSAWAED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1054 TSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIM----EALQYLHNCRVAHLDIKPENLLIDlRIPVPRVKLIDLE 1129
Cdd:cd14138   78 DHMLIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLlqvaRGLKYIHSMSLVHMDIKPSNIFIS-RTSIPNAASEEGD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1130 DAVQISGH--FHIHHL-----LGNPE-------FAAPEVIQGIPVSLG-TDIWSIGvLTYVMLSGVSPFL---DESKEET 1191
Cdd:cd14138  157 EDEWASNKviFKIGDLghvtrVSSPQveegdsrFLANEVLQENYTHLPkADIFALA-LTVVCAAGAEPLPtngDQWHEIR 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1192 CINVCRVDFSFPHEYFcgvsnaarDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd14138  236 QGKLPRIPQVLSQEFL--------DLLKVMIHPDPERRPSAVALVKHS 275
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
773-868 1.41e-09

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 56.05  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  773 APEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITW--KGPD-QNILDTDnssatytvSSCDSGEITLKICNLMPQDSGIY 849
Cdd:cd20972    1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWfcEGKElQNSPDIQ--------IHQEGDLHSLIIAEAFEEDTGRY 72
                         90
                 ....*....|....*....
gi 68362740  850 TCIATNDHGTTSTSATVKV 868
Cdd:cd20972   73 SCLATNSVGSDTTSAEIFV 91
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
992-1197 1.42e-09

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: 60.29  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYIlILELMDDGRLLDY 1071
Cdd:cd05067   14 RLGAGQFGEVWMGYYNGHTK-VAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYI-ITEYMENGSLVDF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHD--ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIP-------VPRVkLIDLEDAVQISGHFHIhh 1142
Cdd:cd05067   92 LKTPSgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSckiadfgLARL-IEDNEYTAREGAKFPI-- 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1143 llgnpEFAAPEVIQGIPVSLGTDIWSIGV-LTYVMLSGVSPFLDESKEETCINVCR 1197
Cdd:cd05067  169 -----KWTAPEAINYGTFTIKSDVWSFGIlLTEIVTHGRIPYPGMTNPEVIQNLER 219
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
986-1240 1.49e-09

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: 60.62  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  986 AYTELNEIGRGRFSIVKKCIHKATRKDVAVK---FVSKKMKKKEQAAHEAALLQHLQHPQYIT----LHDTYESPTSYI- 1057
Cdd:cd07837    2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKktrLEMEEEGVPSTALREVSLLQMLSQSIYIVrlldVEHVEENGKPLLy 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDG--RLLDYLM--NHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQ 1133
Cdd:cd07837   82 LVFEYLDTDlkKFIDSYGrgPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLKIADLGLGRAFT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1134 ISGHFHIHHLLgNPEFAAPEVIQG-IPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSN 1212
Cdd:cd07837  162 IPIKSYTHEIV-TLWYRAPEVLLGsTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEVWPGVSK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1213 ------------------------AARDFINVILQEDFRRRPTAATCLQHPW 1240
Cdd:cd07837  241 lrdwheypqwkpqdlsravpdlepEGVDLLTKMLAYDPAKRISAKAALQHPY 292
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
990-1184 1.69e-09

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: 60.47  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHK----ATRKDVAVKF--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESP--TSYILILE 1061
Cdd:cd05038    9 IKQLGEGHFGSVELCRYDplgdNTGEQVAVKSlqPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAV-QISGH 1137
Cdd:cd05038   89 YLPSGSLRDYLQRHrDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESE---DLVKISDfgLAKVLpEDKEY 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 68362740 1138 FHIHHLLGNPEF-AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFL 1184
Cdd:cd05038  166 YYVKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
786-868 1.79e-09

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 55.94  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  786 LLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSATYTVSSCDSGEITLKicnlmpqDSGIYTCIATNDHGTTSTSAT 865
Cdd:cd05764   13 LEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDNGTLDILITTVK-------DTGAFTCIASNPAGEATARVE 85

                 ...
gi 68362740  866 VKV 868
Cdd:cd05764   86 LHI 88
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
1004-1179 1.88e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 61.16  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1004 CIHKATRKDVAVKfvskkMKKKEQAAHEAALLQHLQHPQYITLHDT--YESPTSYILILELMDdgrLLDYLMNHDELMEE 1081
Cdd:PHA03212  111 CIDNKTCEHVVIK-----AGQRGGTATEAHILRAINHPSIIQLKGTftYNKFTCLILPRYKTD---LYCYLAAKRNIAIC 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1082 KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLripvP-RVKLIDLEDA---VQISGHFHiHHLLGNPEFAAPEVIQG 1157
Cdd:PHA03212  183 DILAIERSVLRAIQYLHENRIIHRDIKAENIFINH----PgDVCLGDFGAAcfpVDINANKY-YGWAGTIATNAPELLAR 257
                         170       180
                  ....*....|....*....|..
gi 68362740  1158 IPVSLGTDIWSIGVLTYVMLSG 1179
Cdd:PHA03212  258 DPYGPAVDIWSAGIVLFEMATC 279
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
989-1239 2.01e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 60.11  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNEIGRGRFSIVKKCIH---------KATRKDVAvKFVSKKMKKKEQAAHeaALLQHlqHPQYITLHDTYESPTSYILI 1059
Cdd:cd14051    4 EVEKIGSGEFGSVYKCINrldgcvyaiKKSKKPVA-GSVDEQNALNEVYAH--AVLGK--HPHVVRYYSAWAEDDHMIIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLLDYLMNH---DELMEE-KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlripvprvKLIDLEDAVQIS 1135
Cdd:cd14051   79 NEYCNGGSLADAISENekaGERFSEaELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFIS--------RTPNPVSSEEEE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1136 GHFHIHHL-------------LG------NPE-------FAAPEVIQGIPVSL-GTDIWSIGvLTYVMLSGVSPFLDESK 1188
Cdd:cd14051  151 EDFEGEEDnpesnevtykigdLGhvtsisNPQveegdcrFLANEILQENYSHLpKADIFALA-LTVYEAAGGGPLPKNGD 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1189 EETCINvcrvDFSFPheYFCGVSNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd14051  230 EWHEIR----QGNLP--PLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
991-1189 2.10e-09

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: 60.21  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVKKCIHKAtrKDVAVKFV-----SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd14158   21 NKLGEGGFGVVFKGYIND--KNVAVKKLaamvdISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDEL------MEEKVAfyiRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpVPRVKLIDLEDA-VQISGHF 1138
Cdd:cd14158   99 GSLLDRLACLNDTpplswhMRCKIA---QGTANGINYLHENNHIHRDIKSANILLDETF-VPKISDFGLARAsEKFSQTI 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1139 HIHHLLGNPEFAAPEVIQGiPVSLGTDIWSIGVLTYVMLSGVSPFlDESKE 1189
Cdd:cd14158  175 MTERIVGTTAYMAPEALRG-EITPKSDIFSFGVVLLEIITGLPPV-DENRD 223
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
980-1238 2.28e-09

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: 60.04  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  980 KENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK-EQAAHEAALLQHLQHPQYITLHDTYESPTSYIL 1058
Cdd:cd06646    4 RRNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDfSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1059 ILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHF 1138
Cdd:cd06646   84 CMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDN---GDVKLADFGVAAKITATI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1139 HIHH-LLGNPEFAAPEViQGIPVSLG----TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPH-EYFCGVSN 1212
Cdd:cd06646  161 AKRKsFIGTPYWMAPEV-AAVEKNGGynqlCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPKlKDKTKWSS 239
                        250       260
                 ....*....|....*....|....*.
gi 68362740 1213 AARDFINVILQEDFRRRPTAATCLQH 1238
Cdd:cd06646  240 TFHNFVKISLTKNPKKRPTAERLLTH 265
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
987-1177 2.65e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 60.49  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS---KKMKKKEQAAHEAALLQHLQHPQYITL------HDTYESPTSYI 1057
Cdd:cd07874   19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSrpfQNQTHAKRAYRELVLMKCVNHKNIISLlnvftpQKSLEEFQDVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMnhdELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPvprVKLIDLEDAVQISGH 1137
Cdd:cd07874   99 LVMELMDANLCQVIQM---ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT---LKILDFGLARTAGTS 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVML 1177
Cdd:cd07874  173 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMV 212
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
981-1183 2.85e-09

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: 59.67  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  981 ENFDSAYTELNE-IGRGRFSIVKKCIHKAtrKDVAVKFV-----SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPT 1054
Cdd:cd14145    1 LEIDFSELVLEEiIGIGGFGKVYRAIWIG--DEVAVKAArhdpdEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 SYILILELMDDGRLlDYLMNHDELMEEKVAFYIRDIMEALQYLHN---CRVAHLDIKPENLLIdlripVPRVKLIDLEDA 1131
Cdd:cd14145   79 NLCLVMEFARGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILI-----LEKVENGDLSNK 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1132 VQISGHFHI----HHLL-----GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14145  153 ILKITDFGLarewHRTTkmsaaGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
990-1178 3.03e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 59.64  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKC----IHKATRKDVAVKFVSKKMKKK-EQAAHEAALLQHLQHPQYITLHDTYESP--TSYILILEL 1062
Cdd:cd14205    9 LQQLGKGNFGSVEMCrydpLQDNTGEVVAVKKLQHSTEEHlRDFEREIEILKSLQHDNIVKYKGVCYSAgrRNLRLIMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELME-EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDL---EDAVQISGHF 1138
Cdd:cd14205   89 LPYGSLRDYLQKHKERIDhIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENEN---RVKIGDFgltKVLPQDKEYY 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1139 HIHHLLGNPEF-AAPEVIQGIPVSLGTDIWSIGVLTYVMLS 1178
Cdd:cd14205  166 KVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYELFT 206
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
987-1272 3.24e-09

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: 60.18  E-value: 3.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAH---EAALLQHLQHPQYITLHDTYESPTS------YI 1057
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRilrEIKLLRLLRHPDIVEIKHIMLPPSRrefkdiYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 lILELMDDGrLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLID----LRI---PVPRVKLIDLED 1130
Cdd:cd07859   82 -VFELMESD-LHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANadckLKIcdfGLARVAFNDTPT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1131 AVQISGHfhihhlLGNPEFAAPEVIQGI--PVSLGTDIWSIGVLTYVMLSG---------------VSPFLDESKEETC- 1192
Cdd:cd07859  160 AIFWTDY------VATRWYRAPELCGSFfsKYTPAIDIWSIGCIFAEVLTGkplfpgknvvhqldlITDLLGTPSPETIs 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1193 ----------INVCRVDFSFP-HEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWL--------QPHNGSYSKIPL 1253
Cdd:cd07859  234 rvrnekarryLSSMRKKQPVPfSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFkglakverEPSAQPITKLEF 313
                        330
                 ....*....|....*....
gi 68362740 1254 DtsrlacFIERRKHQNDVR 1272
Cdd:cd07859  314 E------FERRRLTKEDVR 326
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
991-1190 3.35e-09

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 59.31  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIV-KKCIHKATRK--DVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05033   10 KVIGGGEFGEVcSGSLKLPGKKeiDVAIKTLKSGYSDKQRLDflTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDE-LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPVPRVKLI----DLEDAVQISGhf 1138
Cdd:cd05033   90 GSLDKFLRENDGkFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVnsDLVCKVSDFGLSrrleDSEATYTTKG-- 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1139 hihhllGN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTY-VMLSGVSPFLDESKEE 1190
Cdd:cd05033  168 ------GKiPiRWTAPEAIAYRKFTSASDVWSFGIVMWeVMSYGERPYWDMSNQD 216
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
987-1191 3.71e-09

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: 58.99  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKdVAVKFV-SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDD 1065
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWKNRVR-VAIKILkSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlripvprvklidlEDAVQISGHFHIHHL 1143
Cdd:cd05148   87 GSLLAFLRSPEGqvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVG-------------EDLVCKVADFGLARL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1144 LGNP-----------EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEET 1191
Cdd:cd05148  154 IKEDvylssdkkipyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEV 213
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
788-858 3.86e-09

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 55.25  E-value: 3.86e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740  788 GDTVILQCKVCGRPKPTITWK----GPDQNILDTDNSSATYTVSSCDSgeitLKICNLMPQDSGIYTCIATNDHG 858
Cdd:cd05765   15 GETASFHCDVTGRPQPEITWEkqvpGKENLIMRPNHVRGNVVVTNIGQ----LVIYNAQPQDAGLYTCTARNSGG 85
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
987-1183 4.91e-09

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: 58.67  E-value: 4.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSivkkCIHKATRKDVAVKFVSKKMKKKEQAA----------------HEAALL-QHLQHPQYITLHDT 1049
Cdd:cd08528    2 YAVLELLGSGAFG----CVYKVRKKSNGQTLLALKEINMTNPAfgrteqerdksvgdiiSEVNIIkEQLRHPNIVRYYKT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1050 Y-ESPTSYIlILELMDDGRLLDYLMN----HDELMEEKVAFYIRDIMEALQYLHNCR-VAHLDIKPENLLIDLRipvPRV 1123
Cdd:cd08528   78 FlENDRLYI-VMELIEGAPLGEHFSSlkekNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGED---DKV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68362740 1124 KLIDLEDAVQ-ISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd08528  154 TITDFGLAKQkGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPF 214
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
779-868 4.96e-09

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 54.82  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  779 PLVDVTCLLGDTVILQCKVCGRPKPTITWKgPDQNILDTDNSSatYTVSScdSGEiTLKICNLMPQDSGIYTCIATND-H 857
Cdd:cd20970    8 PSFTVTAREGENATFMCRAEGSPEPEISWT-RNGNLIIEFNTR--YIVRE--NGT-TLTIRNIRRSDMGIYLCIASNGvP 81
                         90
                 ....*....|.
gi 68362740  858 GTTSTSATVKV 868
Cdd:cd20970   82 GSVEKRITLQV 92
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
993-1230 5.60e-09

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 58.83  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKAT-RKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd05063   13 IGAGEFGEVFRGILKMPgRKEVAVAIKTLKPGYTEKQRQdflsEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIP-------VPRVKLIDLEDAVQISGhfh 1139
Cdd:cd05063   93 LDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLEckvsdfgLSRVLEDDPEGTYTTSG--- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 ihhllGN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTY-VMLSGVSPFLDESKEETcINVCRVDFSFPHEYFCgvSNAARD 1216
Cdd:cd05063  170 -----GKiPiRWTAPEAIAYRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEV-MKAINDGFRLPAPMDC--PSAVYQ 241
                        250
                 ....*....|....
gi 68362740 1217 FINVILQEDFRRRP 1230
Cdd:cd05063  242 LMLQCWQQDRARRP 255
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
1079-1238 7.12e-09

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: 58.57  E-value: 7.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1079 MEEKVAFYirDIMEALQYLHNCRVAHLDIKPENLLIDLRipvprvklidlEDAVQISGHFHIHHLL----------GNPE 1148
Cdd:cd13974  132 REALVIFY--DVVRVVEALHKKNIVHRDLKLGNMVLNKR-----------TRKITITNFCLGKHLVseddllkdqrGSPA 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1149 FAAPEVIQGIPVsLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYfcGVSNAARDFINVILQEDF 1226
Cdd:cd13974  199 YISPDVLSGKPY-LGkpSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDG--RVSENTVCLIRKLLVLNP 275
                        170
                 ....*....|..
gi 68362740 1227 RRRPTAATCLQH 1238
Cdd:cd13974  276 QKRLTASEVLDS 287
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
987-1179 7.76e-09

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: 58.96  E-value: 7.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS---KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSY------I 1057
Cdd:cd07850    2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpfQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDdGRLLDYLmnHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVprvKLIDLEDAVQISGH 1137
Cdd:cd07850   82 LVMELMD-ANLCQVI--QMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTL---KILDFGLARTAGTS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSG 1179
Cdd:cd07850  156 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRG 197
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
987-1239 9.62e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 58.02  E-value: 9.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVK--FVSKKMKKKEQAA-HEA---ALLQHlqHPQYITLHDTYESPTSYILIL 1060
Cdd:cd14139    2 FLELEKIGVGEFGSVYKCIKRLDGCVYAIKrsMRPFAGSSNEQLAlHEVyahAVLGH--HPHVVRYYSAWAEDDHMIIQN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDDGRLLDYLMNHDELMEEKVAFYIRDIM----EALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISG 1136
Cdd:cd14139   80 EYCNGGSLQDAISENTKSGNHFEEPELKDILlqvsMGLKYIHNSGLVHLDIKPSNIFICHKMQSSSGVGEEVSNEEDEFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIHHLLG---------NPE-------FAAPEVIQGIPVSL-GTDIWSIGvLTYVMLSGVSPFLDESKEETCINVCRVD 1199
Cdd:cd14139  160 SANVVYKIGdlghvtsinKPQveegdsrFLANEILQEDYRHLpKADIFALG-LTVALAAGAEPLPTNGAAWHHIRKGNFP 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 68362740 1200 fSFPHEyfcgVSNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:cd14139  239 -DVPQE----LPESFSSLLKNMIQPDPEQRPSATALARHT 273
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
1027-1195 1.12e-08

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: 58.90  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1027 QAAH---EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVA 1103
Cdd:cd05625   44 QVAHvkaERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1104 HLDIKPENLLIDLRipvPRVKLIDL----------------------EDAVQISGHFH---------------------- 1139
Cdd:cd05625  124 HRDIKPDNILIDRD---GHIKLTDFglctgfrwthdskyyqsgdhlrQDSMDFSNEWGdpencrcgdrlkplerraarqh 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 ----IHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINV 1195
Cdd:cd05625  201 qrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKV 260
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
993-1183 1.17e-08

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: 57.74  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKAtrKDVAVKFV-----SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGR 1067
Cdd:cd14146    2 IGVGGFGKVYRATWKG--QEVAVKAArqdpdEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELMEEKVAFYIR---------DIMEALQYLHN---CRVAHLDIKPENLLIDLRIPVPRV--KLIDLEDaVQ 1133
Cdd:cd14146   80 LNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEeavVPILHRDLKSSNILLLEKIEHDDIcnKTLKITD-FG 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 68362740 1134 ISGHFHIHHLL---GNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14146  159 LAREWHRTTKMsaaGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
987-1189 1.20e-08

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 58.32  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCI-HKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP------QYITLHDTYESPTSYILI 1059
Cdd:cd14213   14 YEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTdpnstfRCVQMLEWFDHHGHVCIV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELM--------DDGRLLDYLMNHDELMEEKvafyirdIMEALQYLHNCRVAHLDIKPENLLI---------------DL 1116
Cdd:cd14213   94 FELLglstydfiKENSFLPFPIDHIRNMAYQ-------ICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpkmkrDE 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68362740 1117 R-IPVPRVKLIDLEDAVqisgHFHIHH--LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPF-LDESKE 1189
Cdd:cd14213  167 RtLKNPDIKVVDFGSAT----YDDEHHstLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFqTHDSKE 239
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
987-1193 1.34e-08

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: 58.60  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHP------QYITLHDTYESPTSYILIL 1060
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNHICMTF 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1061 ELMDdgrlldylMNHDELMEEK---------VAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPR--VKLIDLE 1129
Cdd:cd14224  147 ELLS--------MNLYELIKKNkfqgfslqlVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQ---GRsgIKVIDFG 215
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1130 DAVqiSGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSG--VSPFLDESKEETCI 1193
Cdd:cd14224  216 SSC--YEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGypLFPGEDEGDQLACM 279
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
993-1187 1.48e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 59.04  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740   993 IGRGRFSIVkkciHKA--TR--KDVAVKFVSKKMKKKEQA-------AHEAAllqHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:NF033483   15 IGRGGMAEV----YLAkdTRldRDVAVKVLRPDLARDPEFvarfrreAQSAA---SLSHPNIVSVYDVGEDGGIPYIVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1062 LMDdGRLL-DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGH--F 1138
Cdd:NF033483   88 YVD-GRTLkDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDFGIARALSSTtmT 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 68362740  1139 HIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDES 1187
Cdd:NF033483  164 QTNSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDS 212
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
992-1184 1.76e-08

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: 56.89  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIH--KATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESpTSYILILELMDDG 1066
Cdd:cd05116    2 ELGSGNFGTVKKGYYqmKKVVKTVAVKILkneANDPALKDELLREANVMQQLDNPYIVRMIGICEA-ESWMLVMEMAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1067 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLID--LEDAVQISGHFHIHHLL 1144
Cdd:cd05116   81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLL---VTQHYAKISDfgLSKALRADENYYKAQTH 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1145 GN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFL 1184
Cdd:cd05116  158 GKwPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYK 200
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
992-1190 1.94e-08

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: 56.96  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYIlILELMDDGRLLDY 1071
Cdd:cd05073   18 KLGAGQFGEVWMATYNKHTK-VAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYI-ITEFMAKGSLLDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHD--ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRI-------PVPRVkLIDLEDAVQISGHFHIhh 1142
Cdd:cd05073   96 LKSDEgsKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLvckiadfGLARV-IEDNEYTAREGAKFPI-- 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 68362740 1143 llgnpEFAAPEVIQGIPVSLGTDIWSIGV-LTYVMLSGVSPFLDESKEE 1190
Cdd:cd05073  173 -----KWTAPEAINFGSFTIKSDVWSFGIlLMEIVTYGRIPYPGMSNPE 216
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
987-1241 1.95e-08

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: 57.80  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKD--VAVKFVS---KKMKKKEQAAHEAALLQHLQ-HPQYITLHD----TYESPTSY 1056
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEetVAIKKITnvfSKKILAKRALRELKLLRHFRgHKNITCLYDmdivFPGNFNEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDdGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDL-------E 1129
Cdd:cd07857   82 YLYEELME-ADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADC---ELKICDFglargfsE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1130 DAVQISGhfHIHHLLGNPEFAAPEVIQGI-PVSLGTDIWSIGVLTYVMLSGVSPF---------------LDESKEETCI 1193
Cdd:cd07857  158 NPGENAG--FMTEYVATRWYRAPEIMLSFqSYTKAIDVWSVGCILAELLGRKPVFkgkdyvdqlnqilqvLGTPDEETLS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1194 ---------------NVCRVDF--SFPheyfcGVSNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd07857  236 rigspkaqnyirslpNIPKKPFesIFP-----NANPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
993-1241 2.24e-08

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: 56.56  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALlqhlQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACF----RHENIAELYGALLWEETVHLFMEAGEGGSVLEKL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLidlrIPVPRVKLIDLEDAVQISGHFHI-HHLLGNPEFAA 1151
Cdd:cd13995   88 ESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIV----FMSTKAVLVDFGLSVQMTEDVYVpKDLRGTEIYMS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1152 PEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLD---ESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRR 1228
Cdd:cd13995  164 PEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRrypRSAYPSYLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNH 243
                        250
                 ....*....|...
gi 68362740 1229 RPTAATCLQHPWL 1241
Cdd:cd13995  244 RSSAAELLKHEAL 256
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
987-1179 2.66e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 57.36  E-value: 2.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS---KKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSY------I 1057
Cdd:cd07875   26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSrpfQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefqdvY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMnhdELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPvprVKLIDLEDAVQISGH 1137
Cdd:cd07875  106 IVMELMDANLCQVIQM---ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCT---LKILDFGLARTAGTS 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 68362740 1138 FHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSG 1179
Cdd:cd07875  180 FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKG 221
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
787-868 2.70e-08

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 52.22  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  787 LGDTVILQCKVCGRPKPTITWKGPDQnILDTDNSSATytvsscDSGEitLKICNLMPQDSGIYTCIATNDHGTTSTSATV 866
Cdd:cd05728   13 IGSSLRWECKASGNPRPAYRWLKNGQ-PLASENRIEV------EAGD--LRITKLSLSDSGMYQCVAENKHGTIYASAEL 83

                 ..
gi 68362740  867 KV 868
Cdd:cd05728   84 AV 85
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
987-1190 2.79e-08

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 57.18  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVS-KKMKKKEQAAHEAALLQHLQ--HPQYITLHDT-------------- 1049
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcNAPENVELALREFWALSSIQrqHPNVIQLEECvlqrdglaqrmshg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1050 ----------------------YESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRdIMEALQYLHNCRVAHLDI 1107
Cdd:cd13977   82 ssksdlylllvetslkgercfdPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQ-LSSALAFLHRNQIVHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1108 KPENLLIDLRIPVPRVKLIDL-------------EDAVQISGHFhIHHLLGNPEFAAPEVIQGiPVSLGTDIWSIGVLTY 1174
Cdd:cd13977  161 KPDNILISHKRGEPILKVADFglskvcsgsglnpEEPANVNKHF-LSSACGSDFYMAPEVWEG-HYTAKADIFALGIIIW 238
                        250
                 ....*....|....*..
gi 68362740 1175 VMLSGVSpFLD-ESKEE 1190
Cdd:cd13977  239 AMVERIT-FRDgETKKE 254
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
779-869 2.81e-08

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 52.24  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  779 PLVDVTCLLGDTVILQCKVCGRPKPTITWkgpdqnILDTDNSSATYTVSSCDSGeiTLKICNLMPQDSGIYTCIATNDHG 858
Cdd:cd20968    5 PPTNVTIIEGLKAVLPCTTMGNPKPSVSW------IKGDDLIKENNRIAVLESG--SLRIHNVQKEDAGQYRCVAKNSLG 76
                         90
                 ....*....|..
gi 68362740  859 TT-STSATVKVQ 869
Cdd:cd20968   77 IAySKPVTIEVE 88
pknD PRK13184
serine/threonine-protein kinase PknD;
1090-1183 2.90e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 58.24  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1090 IMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRV-----KLIDLEDAVQISGHFHI----HH-------LLGNPEFAAPE 1153
Cdd:PRK13184  122 ICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILdwgaaIFKKLEEEDLLDIDVDErnicYSsmtipgkIVGTPDYMAPE 201
                          90       100       110
                  ....*....|....*....|....*....|
gi 68362740  1154 VIQGIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:PRK13184  202 RLLGVPASESTDIYALGVILYQMLTLSFPY 231
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
987-1115 2.91e-08

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: 56.67  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELM 1063
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEgvpSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1064 DDG--RLLDYLmnHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLID 1115
Cdd:cd07839   82 DQDlkKYFDSC--NGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN 133
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
993-1172 3.41e-08

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: 56.49  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVK-FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDL------------RIPVPRVKLIDLEDAVQISGHFH 1139
Cdd:cd14222   81 LRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLdktvvvadfglsRLIVEEKKKPPPDKPTTKKRTLR 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 68362740 1140 I------HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVL 1172
Cdd:cd14222  161 KndrkkrYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIV 199
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
788-868 3.78e-08

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 52.01  E-value: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  788 GDTVILQCKVCGRPKPTITWKGPDQNILdTDNSSATYTVSScdsgEITLKICNLMPQDSGIYTCIATNDHGTTSTSATVK 867
Cdd:cd20969   17 GHTVQFVCRADGDPPPAILWLSPRKHLV-SAKSNGRLTVFP----DGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLH 91

                 .
gi 68362740  868 V 868
Cdd:cd20969   92 V 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
799-868 4.31e-08

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 51.44  E-value: 4.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68362740  799 GRPKPTITWKGPDQNILDTD----NSSATYTVsscdsgeITLKICNlmPQDSGIYTCIATNDHGTTSTSATVKV 868
Cdd:cd05748   18 GRPTPTVTWSKDGQPLKETGrvqiETTASSTS-------LVIKNAK--RSDSGKYTLTLKNSAGEKSATINVKV 82
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
983-1241 6.47e-08

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 56.19  E-value: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  983 FDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQhlqhpqyiTLHDTYESPTSYILILEL 1062
Cdd:cd14217   10 FNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLR--------CVRESDPEDPNKDMVVQL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGR-------------------LLDYLM--NHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLI---DLR 1117
Cdd:cd14217   82 IDDFKisgmngihvcmvfevlghhLLKWIIksNYQGLPIRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILMcvdDAY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1118 I---------------PVP------------------------RVKLIDLEDAVQIsgHFHIHHLLGNPEFAAPEVIQGI 1158
Cdd:cd14217  162 VrrmaaeatewqkagaPPPsgsavstapdllvnpldprnadkiRVKIADLGNACWV--HKHFTEDIQTRQYRSIEVLIGA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1159 PVSLGTDIWSIGVLTYVMLSGVSPF-----LDESKEETCINV-----------CRVDFSFPHEYFC-------------- 1208
Cdd:cd14217  240 GYSTPADIWSTACMAFELATGDYLFephsgEDYSRDEDHIAHiiellgciprhFALSGKYSREFFNrrgelrhitklkpw 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1209 ------------GVSNAAR--DFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14217  320 slfdvlvekygwPHEDAAQftDFLIPMLEMVPEKRASAGECLRHPWL 366
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
1066-1241 6.61e-08

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: 54.88  E-value: 6.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1066 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGH---FHIHH 1142
Cdd:cd14024   69 GDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRT-KLVLVNLEDSCPLNGDddsLTDKH 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 llGNPEFAAPEVIQGIPVSLG--TDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHeyfcGVSNAARDFINV 1220
Cdd:cd14024  148 --GCPAYVGPEILSSRRSYSGkaADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPA----WLSPGARCLVSC 221
                        170       180
                 ....*....|....*....|.
gi 68362740 1221 ILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14024  222 MLRRSPAERLKASEILLHPWL 242
SH3_Kalirin_1 cd11852
First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or ...
631-686 6.82e-08

First Src homology 3 domain of the RhoGEF kinase, Kalirin; Kalirin, also called Duo, Duet, or TRAD, is a large neuronal dual Rho guanine nucleotide exchange factor (RhoGEF) that activates Rac1, RhoA, and RhoG using two RhoGEF domains. Kalirin exists in many isoforms generated by alternative splicing and the use of multiple promoters; the major isoforms are kalirin-7, -9, and -12, which differ at their C-terminal ends. Kalirin-12, the longest isoform, contains an N-terminal Sec14p domain, spectrin-like repeats, two RhoGEF domains, two SH3 domains, as well as Ig, FNIII, and kinase domains at the C-terminal end. Kalirin-7 contains only a single RhoGEF domain and does not contain an SH3 domain. Kalirin, through its many isoforms, interacts with many different proteins and is able to localize to different locations within the cell. It influences neurite initiation, axon growth, dendritic morphogenesis, vesicle trafficking, neuronal maintenance, and neurodegeneration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212786  Cd Length: 62  Bit Score: 50.47  E-value: 6.82e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740  631 VIKDYYALKENEICVSQGEVVQVL--AVNQQNMCLVYQPASDHSPAAEGWVPGSILAP 686
Cdd:cd11852    5 VIEDFEATSSQELTVSKGQTVEVLerPSSRPDWCLVRTLEQDNSPPQEGLVPSSILCI 62
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
1057-1241 7.02e-08

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 54.92  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1057 ILILELMDDGRLLDYLMnhdELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipVPRVKLIDLEDAVQISG 1136
Cdd:cd14019   80 VAVLPYIEHDDFRDFYR---KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRE--TGKGVLVDFGLAQREED 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1137 HFHIH-HLLGNPEFAAPEVI-----QGIPVslgtDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSfpheyfcgv 1210
Cdd:cd14019  155 RPEQRaPRAGTRGFRAPEVLfkcphQTTAI----DIWSAGVILLSILSGRFPFFFSSDDIDALAEIATIFG--------- 221
                        170       180       190
                 ....*....|....*....|....*....|.
gi 68362740 1211 SNAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14019  222 SDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
996-1194 7.81e-08

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: 55.20  E-value: 7.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  996 GRFSIVKKCIHKaTRKDVAVKFVSKKMKKKEQAA---HEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYL 1072
Cdd:cd14027    4 GGFGKVSLCFHR-TQGLVVLKTVYTGPNCIEHNEallEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1073 MNHDELMEEKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLID--LRIPVPRV---------KLIDLEDAVQISGHFHIH 1141
Cdd:cd14027   83 KKVSVPLSVKGRI-ILEIIEGMAYLHGKGVIHKDLKPENILVDndFHIKIADLglasfkmwsKLTKEEHNEQREVDGTAK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1142 HLLGNPEFAAPEVIQGIPV--SLGTDIWSIGVLTYVMLSGVSPFldeskeETCIN 1194
Cdd:cd14027  162 KNAGTLYYMAPEHLNDVNAkpTEKSDVYSFAIVLWAIFANKEPY------ENAIN 210
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
993-1183 8.63e-08

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: 54.99  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRkdVAVKFVSKKMKKKEQAAhEAALLQHLQHPQYITLHDT-YESPTSYILILELMDDGRLLDY 1071
Cdd:cd05082   14 IGKGEFGDVMLGDYRGNK--VAVKCIKNDATAQAFLA-EASVMTQLRHSNLVQLLGViVEEKGGLYIVTEYMAKGSLVDY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPVPRVKLIDLEDAVQISGHFHIhhllgnp 1147
Cdd:cd05082   91 LRSRGRsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVseDNVAKVSDFGLTKEASSTQDTGKLPV------- 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 68362740 1148 EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPF 1183
Cdd:cd05082  164 KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
1001-1237 1.13e-07

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 55.10  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1001 VKKcIHKATRKDVAVKFvskkmkkKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILIleLMDDG--RLLDYLMNHDEL 1078
Cdd:cd14001   33 VKK-INSKCDKGQRSLY-------QERLKEEAKILKSLNHPNIVGFRAFTKSEDGSLCL--AMEYGgkSLNDLIEERYEA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1079 MEE--------KVAFyirDIMEALQYLHN-CRVAHLDIKPENLLI--DLRIpvprVKLIDLEDAVQISGHFHIH-----H 1142
Cdd:cd14001  103 GLGpfpaatilKVAL---SIARALEYLHNeKKILHGDIKSGNVLIkgDFES----VKLCDFGVSLPLTENLEVDsdpkaQ 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1143 LLGNPEFAAPEVI-QGIPVSLGTDIWSIGVLTYVMLSGVSPFL------DESKEETC-------------------INVC 1196
Cdd:cd14001  176 YVGTEPWKAKEALeEGGVITDKADIFAYGLVLWEMMTLSVPHLnlldieDDDEDESFdedeedeeayygtlgtrpaLNLG 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 68362740 1197 RVDFSFPH--EYFCgvsnaardfinVILQEDFRRRPTAATCLQ 1237
Cdd:cd14001  256 ELDDSYQKviELFY-----------ACTQEDPKDRPSAAHIVE 287
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
1030-1184 1.50e-07

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: 54.59  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1030 HEAALLQHLQHPQYITLHDTYESPTSYILilELMDDGRLLDYLM-NHD--------ELMEEKVAFyirDIMEALQYLHNC 1100
Cdd:cd14067   59 QEASMLHSLQHPCIVYLIGISIHPLCFAL--ELAPLGSLNTVLEeNHKgssfmplgHMLTFKIAY---QIAAGLAYLHKK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1101 RVAHLDIKPENLLI---DLRIPVpRVKLIDLEDAVQiSGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVML 1177
Cdd:cd14067  134 NIIFCDLKSDNILVwslDVQEHI-NIKLSDYGISRQ-SFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELL 211

                 ....*..
gi 68362740 1178 SGVSPFL 1184
Cdd:cd14067  212 SGQRPSL 218
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
989-1203 1.76e-07

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 54.11  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNEIGRGRFSIvkkcihkATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILILELMD 1064
Cdd:cd05065   16 EFGEVCRGRLKL-------PGKREIFVAIKTLKSGYTEKQRRdflsEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1065 DGRLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpVPRVKLIDLEDAVQ--ISGHFHIH 1141
Cdd:cd05065   89 NGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNL-VCKVSDFGLSRFLEddTSDPTYTS 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1142 HLLGN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTY-VMLSGVSPFLDESKEETcINVCRVDFSFP 1203
Cdd:cd05065  168 SLGGKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWeVMSYGERPYWDMSNQDV-INAIEQDYRLP 231
PH_PLEKHG1_G2_G3 cd13243
Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) ...
388-528 1.88e-07

Pleckstrin homology domain-containing family G members 1, 2, and 3 pleckstrin homology (PH) domain; PLEKHG1 (also called ARHGEF41), PLEKHG2 (also called ARHGEF42 or CLG/common-site lymphoma/leukemia guanine nucleotide exchange factor2), and PLEKHG3 (also called ARHGEF43) have RhoGEF DH/double-homology domains in tandem with a PH domain which is involved in phospholipid binding. They function as a guanine nucleotide exchange factor (GEF) and are involved in the regulation of Rho protein signal transduction. Mutations in PLEKHG1 have been associated panic disorder (PD), an anxiety disorder characterized by panic attacks and anticipatory anxiety. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270063 [Multi-domain]  Cd Length: 147  Bit Score: 51.58  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  388 SDIEKAVELMCLVPKRCNDM-------MNLGRLQ----GFEG-TLTAQGKLLQQDTFyvieldaGMQSRTKERRVFLFEQ 455
Cdd:cd13243    2 SVVEEALDTMTQVAWHINDMkrkhehaVRVQEIQslldGWEGpELTTYGDLVLEGTF-------RMAGAKNERLLFLFDK 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68362740  456 IVifseLLRKGSLTPGYMFKRSIKMNYLVLEENVDNDPCKFALMNRETSE-RVVLQAANADIQQAWVQDINQVL 528
Cdd:cd13243   75 ML----LITKKREDGILQYKTHIMCSNLMLSESIPKEPLSFQVLPFDNPKlQYTLQAKNQEQKRLWTQEIKRLI 144
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
987-1115 2.03e-07

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: 54.24  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIHKATRKDVAVKFV---SKKMKKKEQAAHEAALLQHLQHPQYITLHD-TYE-------SPTS 1055
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKIlmhNEKDGFPITALREIKILKKLKHPNVVPLIDmAVErpdkskrKRGS 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740 1056 YILILELMD-DgrLLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLID 1115
Cdd:cd07866   90 VYMVTPYMDhD--LSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILID 149
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
782-869 2.18e-07

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 49.85  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  782 DVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILdtdnSSATYTVSscdsgEITLKICNLMPQDSGIYTCIATNDHGTTS 861
Cdd:cd04968   10 DTYALKGQTVTLECFALGNPVPQIKWRKVDGSPS----SQWEITTS-----EPVLEIPNVQFEDEGTYECEAENSRGKDT 80

                 ....*...
gi 68362740  862 TSATVKVQ 869
Cdd:cd04968   81 VQGRIIVQ 88
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
786-876 2.60e-07

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.


Pssm-ID: 409534  Cd Length: 116  Bit Score: 50.35  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  786 LLGDTVILQCKVCGRPKPTITW----KGPDQNI--------LDTDNSSATYTVSSCDsgeiTLKICNLMPQDSGIYTCIA 853
Cdd:cd20940   13 LVGDSVELHCEAVGSPIPEIQWwfegQEPNEICsqlwdgarLDRVHINATYHQHATS----TISIDNLTEEDTGTYECRA 88
                         90       100
                 ....*....|....*....|...
gi 68362740  854 TNDHGTTSTSATVKVQGVPAAPN 876
Cdd:cd20940   89 SNDPDRNHLTRAPKVKWIRSQAN 111
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
979-1115 2.63e-07

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: 53.91  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  979 WKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQHPQYITLHDTYESPT- 1054
Cdd:cd07865    6 PFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGfpiTALREIKILQLLKHENVVNLIEICRTKAt 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 -------SYILILELM--DDGRLLDYLMNHDELMEEKVAfyIRDIMEALQYLHNCRVAHLDIKPENLLID 1115
Cdd:cd07865   86 pynrykgSIYLVFEFCehDLAGLLSNKNVKFTLSEIKKV--MKMLLNGLYYIHRNKILHRDMKAANILIT 153
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
783-868 2.94e-07

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 49.52  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  783 VTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNssatYTVsSCDSGE-ITLKICNLMPQDSGIYTCIATNDHGTTS 861
Cdd:cd05891   11 VTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEH----YSV-KLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGET 85

                 ....*..
gi 68362740  862 TSATVKV 868
Cdd:cd05891   86 VDVTVSV 92
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
782-868 3.65e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 49.16  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  782 DVTCLLGDTVILQCKVCGRPKPTITWkgpdQNILDTDNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCIATNDHGTTS 861
Cdd:cd05763    8 DITIRAGSTARLECAATGHPTPQIAW----QKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSIS 83

                 ....*..
gi 68362740  862 TSATVKV 868
Cdd:cd05763   84 ANATLTV 90
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
774-868 4.60e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.27  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKgPDQNILDTDNSSATYTVSSCDSGEITLKicNLMPQDSGIYTCIA 853
Cdd:cd20974    1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWF-RDGQVISTSTLPGVQISFSDGRAKLSIP--AVTKANSGRYSLTA 77
                         90
                 ....*....|....*
gi 68362740  854 TNDHGTTSTSATVKV 868
Cdd:cd20974   78 TNGSGQATSTAELLV 92
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
774-868 4.88e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 49.00  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKgpdqnildTDNSSATYTVSSC-----DSGEITLKICNLMPQDSGI 848
Cdd:cd05892    1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWK--------KNNEMLQYNTDRIslyqdNCGRICLLIQNANKKDAGW 72
                         90       100
                 ....*....|....*....|
gi 68362740  849 YTCIATNDHGTTSTSATVKV 868
Cdd:cd05892   73 YTVSAVNEAGVVSCNARLDV 92
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
788-859 4.96e-07

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 48.64  E-value: 4.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68362740  788 GDTVILQCKVCGRPKPTITWK---GPDQnildtdnSSATYTVSScDSGEITLKICNLMPQDSGIYTCIATNDHGT 859
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRlnwGHVP-------DSARVSITS-EGGYGTLTIRDVKESDQGAYTCEAINTRGM 67
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
781-868 5.28e-07

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 48.55  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  781 VDVTCLLGDTVILQCKV-CGRPKPTITWKGPDQNILDTDNSsatytVSSCDSGeiTLKICNLMPQDSGIYTCIATNDHGT 859
Cdd:cd05724    5 SDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNER-----VRIVDDG--NLLIAEARKSDEGTYKCVATNMVGE 77
                         90
                 ....*....|
gi 68362740  860 -TSTSATVKV 868
Cdd:cd05724   78 rESRAARLSV 87
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
992-1121 5.48e-07

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 52.74  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIH---KATRKDVAVKFVSkkmkkkeQA----------AHEAaLLQHLQHPQYITLHDTYESPTSYIL 1058
Cdd:cd13981    7 ELGEGGYASVYLAKDddeQSDGSLVALKVEK-------PPsiwefyicdqLHSR-LKNSRLRESISGAHSAHLFQDESIL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740 1059 ILELMDDGRLLDY--LMNHDEL--MEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVP 1121
Cdd:cd13981   79 VMDYSSQGTLLDVvnKMKNKTGggMDEPLAmFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICAD 146
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
775-871 5.56e-07

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 49.18  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  775 EFLVPLVDVTCLLGDTVILQCKVCGRPKPTITW-KGPDQNIL---DTDNSSATYTVSScdSGEITlkICNLMPQDSGIYT 850
Cdd:cd05726    1 QFVVKPRDQVVALGRTVTFQCETKGNPQPAIFWqKEGSQNLLfpyQPPQPSSRFSVSP--TGDLT--ITNVQRSDVGYYI 76
                         90       100
                 ....*....|....*....|.
gi 68362740  851 CIATNDHGTTSTSATVKVQGV 871
Cdd:cd05726   77 CQALNVAGSILAKAQLEVTDV 97
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
993-1191 6.10e-07

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: 52.06  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKF--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLD 1070
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTcrETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNH-DELMEEKVAFYIRDIMEALQYLH--NCrvAHLDIKPENLLIDLRipvPRVKLIDL------EDAVQI--SGHFH 1139
Cdd:cd05041   83 FLRKKgARLTVKQLLQMCLDAAAGMEYLEskNC--IHRDLAARNCLVGEN---NVLKISDFgmsreeEDGEYTvsDGLKQ 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 68362740 1140 IhhllgnP-EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEET 1191
Cdd:cd05041  158 I------PiKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQT 205
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
788-868 6.92e-07

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 48.46  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  788 GDTVILQCKVCGRPKPTITW-KGPDQNIldtdNSSatyTVSSCDSGeiTLKICNLMPQDSGIYTCIATNDHGTTSTSATV 866
Cdd:cd05852   17 GGRVIIECKPKAAPKPKFSWsKGTELLV----NNS---RISIWDDG--SLEILNITKLDEGSYTCFAENNRGKANSTGVL 87

                 ..
gi 68362740  867 KV 868
Cdd:cd05852   88 SV 89
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
993-1172 8.84e-07

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: 51.75  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKfVSKKMKKKEQAAHEAALLQHLQHPQY-----ITLHDTYESPtsyilILELMDDGR 1067
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVK-IYKNDVDQHKIVREISLLQKLSHPNIvrylgICVKDEKLHP-----ILEYVSGGC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNHDELM--EEKVAFYIrDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQI------SGHFH 1139
Cdd:cd14156   75 LEELLAREELPLswREKVELAC-DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempanDPERK 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 68362740 1140 IhHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVL 1172
Cdd:cd14156  154 L-SLVGSAFWMAPEMLRGEPYDRKVDVFSFGIV 185
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
1029-1241 9.49e-07

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 52.24  E-value: 9.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1029 AHEAALLQHLQ-HPQYITL------HDTYESPTsYILILELMDDG--RLLDYLMN--HDELMEEKVAfyiRDIMEALQYL 1097
Cdd:cd14020   51 AKERAALEQLQgHRNIVTLygvftnHYSANVPS-RCLLLELLDVSvsELLLRSSNqgCSMWMIQHCA---RDVLEALAFL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1098 HNCRVAHLDIKPENLLIDLRIPVprVKLIDLEDAVQiSGHFHIHHLLGNpEFAAPEV-IQ------GIPVSLG----TDI 1166
Cdd:cd14020  127 HHEGYVHADLKPRNILWSAEDEC--FKLIDFGLSFK-EGNQDVKYIQTD-GYRAPEAeLQnclaqaGLQSETEctsaVDL 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1167 WSIGVLTYVMLSGVSpfLDE---SKEETCINVCRVDFSFPHEyfcGVSNAA------RDFINVILQEDFRRRPTAATCLQ 1237
Cdd:cd14020  203 WSLGIVLLEMFSGMK--LKHtvrSQEWKDNSSAIIDHIFASN---AVVNPAipayhlRDLIKSMLHNDPGKRATAEAALC 277

                 ....
gi 68362740 1238 HPWL 1241
Cdd:cd14020  278 SPFF 281
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
788-868 1.06e-06

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 47.97  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  788 GDTVILQCKVCGRPKPTITWKGPDQNILDTDnSSATYTVSSCdsgeiTLKICNLMPQDSGIYTCIATNDHGTTSTSATVK 867
Cdd:cd05867   14 GETARLDCQVEGIPTPNITWSINGAPIEGTD-PDPRRHVSSG-----ALILTDVQPSDTAVYQCEARNRHGNLLANAHVH 87

                 .
gi 68362740  868 V 868
Cdd:cd05867   88 V 88
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
985-1190 1.06e-06

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 51.94  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  985 SAYTELNEIGRGRFSIVKKCIHKAT-----RKDVAVKFVSKKMKKK--EQAAHEAALLQHLQHPQYITLHD--TYESPTS 1055
Cdd:cd05091    6 SAVRFMEELGEDRFGKVYKGHLFGTapgeqTQAVAIKTLKDKAEGPlrEEFRHEAMLRSRLQHPNIVCLLGvvTKEQPMS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1056 yiLILELMDDGRLLDYLM-----------NHDELME---EKVAFY--IRDIMEALQYLHNCRVAHLDIKPENLLIDLRIp 1119
Cdd:cd05091   86 --MIFSYCSHGDLHEFLVmrsphsdvgstDDDKTVKstlEPADFLhiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKL- 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68362740 1120 vpRVKLIDLEDAVQISGHFHiHHLLGNPEFA----APEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPFLDESKEE 1190
Cdd:cd05091  163 --NVKISDLGLFREVYAADY-YKLMGNSLLPirwmSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQD 235
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
993-1183 1.08e-06

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: 52.11  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVKFVSKKMKK--KEQAAHEAALLQHLQHPQYITLHDTYESPTSY--ILILELMDDGRL 1068
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMrpLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRhkVLVMELCPCGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 ---LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRV-KLIDLEDAVQISGHFHIHHLL 1144
Cdd:cd13988   81 ytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAARELEDDEQFVSLY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 68362740 1145 GNPEFAAPEVIQ--------GIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd13988  161 GTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
993-1174 1.09e-06

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: 51.51  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATrKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHD--TYESPTsYIlILELMDDGRLLD 1070
Cdd:cd05034    3 LGAGQFGEVWMGVWNGT-TKVAVKTLKPGTMSPEAFLQEAQIMKKLRHDKLVQLYAvcSDEEPI-YI-VTELMSKGSLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1071 YLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID------LEDAVQISGH---FH 1139
Cdd:cd05034   80 YLRTGEGraLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGEN---NVCKVADfglarlIEDDEYTAREgakFP 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 68362740 1140 IhhllgnpEFAAPEVIQGIPVSLGTDIWSIGVLTY 1174
Cdd:cd05034  157 I-------KWTAPEAALYGRFTIKSDVWSFGILLY 184
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
991-1183 1.10e-06

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 51.65  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  991 NEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHD--TYESPtsYILILELMDDGRL 1068
Cdd:cd05052   12 HKLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGvcTREPP--FYIITEFMPYGNL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1069 LDYLMNHD-ELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHFHIHHllGN 1146
Cdd:cd05052   90 LDYLRECNrEELNAVVLLYMaTQIASAMEYLEKKNFIHRDLAARNCLVG---ENHLVKVADFGLSRLMTGDTYTAH--AG 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 68362740 1147 PEF----AAPEVIQGIPVSLGTDIWSIGVL-----TYvmlsGVSPF 1183
Cdd:cd05052  165 AKFpikwTAPESLAYNKFSIKSDVWAFGVLlweiaTY----GMSPY 206
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
979-1128 1.13e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 52.11  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  979 WKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQHPQYITLH-------- 1047
Cdd:cd07864    1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQLNHRSVVNLKeivtdkqd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1048 --DTYESPTSYILILELMDD---GRLLDYLMNHDElmeEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPR 1122
Cdd:cd07864   81 alDFKKDKGAFYLVFEYMDHdlmGLLESGLVHFSE---DHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK---GQ 154

                 ....*.
gi 68362740 1123 VKLIDL 1128
Cdd:cd07864  155 IKLADF 160
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
987-1172 1.21e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 51.96  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCIH-KATRKDVAVKFVSKKMKKKE---QAAHEAALLQHLQ---HPQYITLHDT-----YESPT 1054
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGmplSTIREVAVLRHLEtfeHPNVVRLFDVctvsrTDRET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1055 SYILILELMDDGrLLDYLMNHDE--LMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdlrIPVPRVKLIDLEDAV 1132
Cdd:cd07862   83 KLTLVFEHVDQD-LTTYLDKVPEpgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV---TSSGQIKLADFGLAR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1133 QISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVL 1172
Cdd:cd07862  159 IYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCI 198
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
1090-1239 1.23e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 52.56  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1090 IMEALQYLHNCRVAHLDIKPENLLIDLRipvprvKLIDLED-------AVQISGHFHiHHLLGNPEFAAPEVIQGIPVSL 1162
Cdd:PTZ00283  152 VLLAVHHVHSKHMIHRDIKSANILLCSN------GLVKLGDfgfskmyAATVSDDVG-RTFCGTPYYVAPEIWRRKPYSK 224
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68362740  1163 GTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFS-FPHEyfcgVSNAARDFINVILQEDFRRRPTAATCLQHP 1239
Cdd:PTZ00283  225 KADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDpLPPS----ISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
781-868 1.29e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 48.00  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  781 VDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSsatYTVSScDSGEITLKicNLMPQDSGIYTCIATNDHGTT 860
Cdd:cd05730   11 VNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEK---YSFNE-DGSEMTIL--DVDKLDEAEYTCIAENKAGEQ 84

                 ....*...
gi 68362740  861 STSATVKV 868
Cdd:cd05730   85 EAEIHLKV 92
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
990-1235 1.38e-06

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: 51.43  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKC----IHKATRKDVAVKFVSKKMKKKEQA-AHEAALLQHLQHPQYITLHDTYESP--TSYILILEL 1062
Cdd:cd05081    9 ISQLGKGNFGSVELCrydpLGDNTGALVAVKQLQHSGPDQQRDfQREIQILKALHSDFIVKYRGVSYGPgrRSLRLVMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1063 MDDGRLLDYLMNHDELMEE-KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLID--LEDAVQISGHFH 1139
Cdd:cd05081   89 LPSGCLRDFLQRHRARLDAsRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESE---AHVKIADfgLAKLLPLDKDYY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1140 IHHLLG-NPEF-AAPEVIQGIPVSLGTDIWSIGVLTYVMLSgvspFLDESKeetcinvcrvdfSFPHEYF--CGVSNAAR 1215
Cdd:cd05081  166 VVREPGqSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFT----YCDKSC------------SPSAEFLrmMGCERDVP 229
                        250       260
                 ....*....|....*....|.
gi 68362740 1216 DFINVI-LQEDFRRRPTAATC 1235
Cdd:cd05081  230 ALCRLLeLLEEGQRLPAPPAC 250
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
1028-1174 1.81e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 52.20  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1028 AAHEAALLQHLQHPQYITLHDTYesPTSYILILELMD-DGRLLDYLMNH-DELMEEKVAFYIRDIMEALQYLHNCRVAHL 1105
Cdd:PHA03211  207 SVHEARLLRRLSHPAVLALLDVR--VVGGLTCLVLPKyRSDLYTYLGARlRPLGLAQVTAVARQLLSAIDYIHGEGIIHR 284
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68362740  1106 DIKPENLLIDlripVPR-VKLIDLEDAVQISGH----FHiHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTY 1174
Cdd:PHA03211  285 DIKTENVLVN----GPEdICLGDFGAACFARGSwstpFH-YGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
1058-1189 1.88e-06

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 51.05  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1058 LILELMDDGRLLDYLMNHDeLMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlRIPVPRVKLIDLEDAVQiSGH 1137
Cdd:cd05080   85 LIMEYVPLGSLRDYLPKHS-IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLD-NDRLVKIGDFGLAKAVP-EGH 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68362740 1138 --FHIHHLLGNPEF-AAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKE 1189
Cdd:cd05080  162 eyYRVREDGDSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTK 216
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
788-868 2.14e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 47.21  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  788 GDTVILQCKVCGRPKPTITW------KGPDQNILDTDNSSATYTvsscdsgeitLKICNLMPQDSGIYTCIATNDHGTTS 861
Cdd:cd05729   19 ANKVRLECGAGGNPMPNITWlkdgkeFKKEHRIGGTKVEEKGWS----------LIIERAIPRDKGKYTCIVENEYGSIN 88

                 ....*..
gi 68362740  862 TSATVKV 868
Cdd:cd05729   89 HTYDVDV 95
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
774-863 2.35e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.02  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNIldtdNSSATYTVSSCDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:cd20990    1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPI----RPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIA 76
                         90
                 ....*....|
gi 68362740  854 TNDHGTTSTS 863
Cdd:cd20990   77 TNRAGQNSFN 86
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
987-1190 2.52e-06

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 51.17  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  987 YTELNEIGRGRFSIVKKCI-HKATRKDVAVKFVSKKMKKKEQAAHEAALLQHL--QHPQY----ITLHDTYESPTSYILI 1059
Cdd:cd14215   14 YEIVSTLGEGTFGRVVQCIdHRRGGARVALKIIKNVEKYKEAARLEINVLEKIneKDPENknlcVQMFDWFDYHGHMCIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1060 LELMDDGRLlDYLMNHDELME--EKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLI-----DLRIPVPR---------- 1122
Cdd:cd14215   94 FELLGLSTF-DFLKENNYLPYpiHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyELTYNLEKkrdersvkst 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68362740 1123 -VKLIDLEDAVqiSGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEE 1190
Cdd:cd14215  173 aIRVVDFGSAT--FDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNRE 239
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
1087-1241 2.82e-06

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 50.90  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1087 IRDIMEALQYLHNCRVAHLDIKPENLLIDlrIPVPRVKLIDLEDAV--QISGHFHIHHLLGNPEFAAPEviQGI------ 1158
Cdd:cd14013  126 MRQILVALRKLHSTGIVHRDVKPQNIIVS--EGDGQFKIIDLGAAAdlRIGINYIPKEFLLDPRYAPPE--QYImstqtp 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1159 -----PVSLGT-------------DIWSIGVLTYVML-------SGVSPFLDESKE-ETCINVCR--VDFSFPHEYFCGV 1210
Cdd:cd14013  202 sappaPVAAALspvlwqmnlpdrfDMYSAGVILLQMAfpnlrsdSNLIAFNRQLKQcDYDLNAWRmlVEPRASADLREGF 281
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 68362740 1211 S------NAARDFINVILQEDFRRRPTAATCLQHPWL 1241
Cdd:cd14013  282 EildlddGAGWDLVTKLIRYKPRGRLSASAALAHPYF 318
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
989-1190 2.91e-06

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 50.54  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  989 ELNEIGRGRFSIVKKCIHKA-----TRKDVAVKFVSKKMKKKEQAA--HEAALLQHLQHPQYITLHDTYESPTSYILILE 1061
Cdd:cd05046    9 EITTLGRGEFGEVFLAKAKGieeegGETLVLVKALQKTKDENLQSEfrRELDMFRKLSHKNVVRLLGLCREAEPHYMILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1062 LMDDGRLLDYLM---NHDELME-------EKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDA 1131
Cdd:cd05046   89 YTDLGDLKQFLRatkSKDEKLKppplstkQKVAL-CTQIALGMDHLSNARFVHRDLAARNCLVSSQREV-KVSLLSLSKD 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1132 VQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTY-VMLSGVSPFLDESKEE 1190
Cdd:cd05046  167 VYNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWeVFTQGELPFYGLSDEE 226
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
773-868 3.11e-06

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the titin-A168169 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409563  Cd Length: 93  Bit Score: 46.69  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  773 APEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNssatYTVSSCDSGEITLKICNL-MPQDSGIYTC 851
Cdd:cd20971    1 APHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGL----KYRIQEFKGGYHQLIIASvTDDDATVYQV 76
                         90
                 ....*....|....*..
gi 68362740  852 IATNDHGTTSTSATVKV 868
Cdd:cd20971   77 RATNQGGSVSGTASLEV 93
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
993-1172 3.72e-06

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: 50.20  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKCIHKATRKDVAVK-FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDY 1071
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKeLIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1072 LMNHDELM--EEKVAFyIRDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPVPRVKLIDLEDA--------VQISGHFH 1139
Cdd:cd14154   81 LKDMARPLpwAQRVRF-AKDIASGMAYLHSMNIIHRDLNSHNCLVreDKTVVVADFGLARLIVEerlpsgnmSPSETLRH 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 68362740 1140 I--------HHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVL 1172
Cdd:cd14154  160 LkspdrkkrYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIV 200
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
1031-1204 3.89e-06

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 50.27  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1031 EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDElmEEKVAFYIR-----DIMEALQYLHN---CRV 1102
Cdd:cd14160   42 ELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLQCHGV--TKPLSWHERiniliGIAKAIHYLHNsqpCTV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1103 AHLDIKPENLLIDLRIpvpRVKLIDLEDA--------------VQISGHFHIHHLlgnPEfaapEVIQGIPVSLGTDIWS 1168
Cdd:cd14160  120 ICGNISSANILLDDQM---QPKLTDFALAhfrphledqsctinMTTALHKHLWYM---PE----EYIRQGKLSVKTDVYS 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 68362740 1169 IGVLTYVMLSGVSPFLDESK------------EETCINVCR--VDFSFPH 1204
Cdd:cd14160  190 FGIVIMEVLTGCKVVLDDPKhlqlrdllhelmEKRGLDSCLsfLDLKFPP 239
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
782-868 3.92e-06

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 46.78  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  782 DVTCLLGDTVILQCKVCGRPKPTITW-KGPDQNILDTDNSSATYTVssCDSGEI-TLKICN--LMPQDSGIYTCIATNDH 857
Cdd:cd07693    9 DLIVSKGDPATLNCKAEGRPTPTIQWlKNGQPLETDKDDPRSHRIV--LPSGSLfFLRVVHgrKGRSDEGVYVCVAHNSL 86
                         90
                 ....*....|..
gi 68362740  858 GT-TSTSATVKV 868
Cdd:cd07693   87 GEaVSRNASLEV 98
PTZ00284 PTZ00284
protein kinase; Provisional
1068-1179 4.01e-06

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 51.12  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  1068 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHN-CRVAHLDIKPENLLI---DLRI---------PVP-RVKLIDLedavq 1133
Cdd:PTZ00284  218 LLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTeLHLMHTDLKPENILMetsDTVVdpvtnralpPDPcRVRICDL----- 292
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 68362740  1134 iSGHFHIHH----LLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSG 1179
Cdd:PTZ00284  293 -GGCCDERHsrtaIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTG 341
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
993-1183 4.02e-06

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: 50.06  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  993 IGRGRFSIVKKcihKATRKDVAVKFVSKKMKKKEQA---AHEAALLQHLQHPQyITLHDTYESPTSYILILELMDDGRLL 1069
Cdd:cd14151   16 IGSGSFGTVYK---GKWHGDVAVKMLNVTAPTPQQLqafKNEVGVLRKTRHVN-ILLFMGYSTKPQLAIVTQWCEGSSLY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1070 DYLMNHDELMEEKVAFYI-RDIMEALQYLHNCRVAHLDIKPENLLI--DLRIPVPRVKLIDLEDavQISGHFHIHHLLGN 1146
Cdd:cd14151   92 HHLHIIETKFEMIKLIDIaRQTAQGMDYLHAKSIIHRDLKSNNIFLheDLTVKIGDFGLATVKS--RWSGSHQFEQLSGS 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1147 PEFAAPEVIQ---GIPVSLGTDIWSIGVLTYVMLSGVSPF 1183
Cdd:cd14151  170 ILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPY 209
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
788-868 4.07e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 46.29  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  788 GDTVILQCKVCGRPKPTITWKgPDQNILDTDNSSATYTVsscDSGEITLKicNLMPQDSGIYTCIATNDHGTTSTSATVK 867
Cdd:cd04978   14 GETGELICEAEGNPQPTITWR-LNGVPIEPAPEDMRRTV---DGRTLIFS--NLQPNDTAVYQCNASNVHGYLLANAFLH 87

                 .
gi 68362740  868 V 868
Cdd:cd04978   88 V 88
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
783-869 4.62e-06

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 46.48  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  783 VTCLLGDTVILQCKVCGRPKpTITWKGPDQNILDTDNSSatYTVSSCDSGEITLKICNLMPQDSGIYTCIATNDHGTTSt 862
Cdd:cd04977   10 AEISVGESKFFLCKVSGDAK-NINWVSPNGEKVLTKHGN--LKVVNHGSVLSSLTIYNANINDAGIYKCVATNGKGTES- 85

                 ....*..
gi 68362740  863 SATVKVQ 869
Cdd:cd04977   86 EATVKLD 92
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
774-868 4.72e-06

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 46.31  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  774 PEFLVPLVDVTCLLGDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSAtytvSSCDSGEITLKICNLMPQDSGIYTCIA 853
Cdd:cd20975    1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFA----EEAEGGLCRLRILAAERGDAGFYTCKA 76
                         90
                 ....*....|....*
gi 68362740  854 TNDHGTTSTSATVKV 868
Cdd:cd20975   77 VNEYGARQCEARLEV 91
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
1031-1190 5.00e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 49.48  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1031 EAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKP 1109
Cdd:cd05066   55 EASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1110 ENLLIDLRI-------PVPRVKLIDLEDAVQISGhfhihhllGN-P-EFAAPEVIQGIPVSLGTDIWSIGVLTY-VMLSG 1179
Cdd:cd05066  135 RNILVNSNLvckvsdfGLSRVLEDDPEAAYTTRG--------GKiPiRWTAPEAIAYRKFTSASDVWSYGIVMWeVMSYG 206
                        170
                 ....*....|.
gi 68362740 1180 VSPFLDESKEE 1190
Cdd:cd05066  207 ERPYWEMSNQD 217
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
787-869 5.31e-06

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 46.19  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  787 LGDTVILQCKVCGRPKPT-ITWKGPDQNILDTDNSSATYTVSSCDSGeiTLKICNLMPQDSGIYTCIATNDHGTTStSAT 865
Cdd:cd05865   14 VGESKFFLCQVAGEAKDKdISWFSPNGEKLTPNQQRISVVRNDDYSS--TLTIYNANIDDAGIYKCVVSNEDEGES-EAT 90

                 ....
gi 68362740  866 VKVQ 869
Cdd:cd05865   91 VNVK 94
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
1013-1195 5.32e-06

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 49.70  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1013 VAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAF-YIRDIM 1091
Cdd:cd13992   28 VAIKHITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSsFIKDIV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1092 EALQYLHNCR-VAHLDIKPENLLIDLRIpvpRVKLID------LEDAVQISGHFHIHH--LLgnpeFAAPEVIQGIP-VS 1161
Cdd:cd13992  108 KGMNYLHSSSiGYHGRLKSSNCLVDSRW---VVKLTDfglrnlLEEQTNHQLDEDAQHkkLL----WTAPELLRGSLlEV 180
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 68362740 1162 LGT---DIWSIGVLTYVMLSGVSPFLDESKEETCINV 1195
Cdd:cd13992  181 RGTqkgDVYSFAIILYEILFRSDPFALEREVAIVEKV 217
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
789-859 5.44e-06

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 46.25  E-value: 5.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68362740  789 DTVILQCKVCGRPKPTITWKgpdQNILDTDNSSATYTVSSCDSGEITLKICNLMPQD-SGIYTCIATNDHGT 859
Cdd:cd05733   17 DNITIKCEAKGNPQPTFRWT---KDGKFFDPAKDPRVSMRRRSGTLVIDNHNGGPEDyQGEYQCYASNELGT 85
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
992-1183 5.65e-06

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: 49.56  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  992 EIGRGRFSIVKKCIHKATRK--DVAVKF--VSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESpTSYILILELMDDGR 1067
Cdd:cd05115   11 ELGSGNFGCVKKGVYKMRKKqiDVAIKVlkQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEA-EALMLVMEMASGGP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLM-NHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEDAVQISGHFHIHHLLGN 1146
Cdd:cd05115   90 LNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL-VNQHYAKISDFGLSKALGADDSYYKARSAGK 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 68362740 1147 -P-EFAAPEVIQGIPVSLGTDIWSIGVLTYVMLS-GVSPF 1183
Cdd:cd05115  169 wPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
990-1174 6.03e-06

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: 49.33  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  990 LNEIGRGRFSIVKKCIHKATRKdVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITLHD--TYESPTsYIlILELMDDGR 1067
Cdd:cd05068   13 LRKLGSGQFGEVWEGLWNNTTP-VAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLYAvcTLEEPI-YI-ITELMKHGS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740 1068 LLDYLMNhdelmeEKVAFYIRDIME-ALQ------YLHNCRVAHLDIKPENLLI-DLRIpvprVKLID--LEDAVQISGH 1137
Cdd:cd05068   90 LLEYLQG------KGRSLQLPQLIDmAAQvasgmaYLESQNYIHRDLAARNVLVgENNI----CKVADfgLARVIKVEDE 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 68362740 1138 FHIHHLLGNP-EFAAPEVIQGIPVSLGTDIWSIGVLTY 1174
Cdd:cd05068  160 YEAREGAKFPiKWTAPEAANYNRFSIKSDVWSFGILLT 197
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
788-868 6.04e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 45.46  E-value: 6.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740    788 GDTVILQCKVCGRPKPTITWKGPDQNILDTDNSSaTYTVSSCDSGeitlkicnlmpqdsgIYTCIATNDHG-TTSTSATV 866
Cdd:pfam13895   14 GEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFF-TLSVSAEDSG---------------TYTCVARNGRGgKVSNPVEL 77

                   ..
gi 68362740    867 KV 868
Cdd:pfam13895   78 TV 79
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
786-869 6.15e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 45.67  E-value: 6.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740  786 LLGDTVILQCKVCGRPKPTITWKGPDqNILDTDNSSATYTvsscdsgEITLKICNLMPQDSGIYTCIATNDHGTTSTSAT 865
Cdd:cd05876    8 LRGQSLVLECIAEGLPTPTVKWLRPS-GPLPPDRVKYQNH-------NKTLQLLNVGESDDGEYVCLAENSLGSARHAYY 79

                 ....
gi 68362740  866 VKVQ 869
Cdd:cd05876   80 VTVE 83
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
433-528 1.12e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 45.62  E-value: 1.12e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68362740     433 YVIELDAGMQSRTKERRVFLFEQIVIFSellRKGSLTPGYMFKRSIKMNYLVLEENVDND----PCKFALMNRETsERVV 508
Cdd:smart00233    6 WLYKKSGGGKKSWKKRYFVLFNSTLLYY---KSKKDKKSYKPKGSIDLSGCTVREAPDPDsskkPHCFEIKTSDR-KTLL 81
                            90       100
                    ....*....|....*....|
gi 68362740     509 LQAANADIQQAWVQDINQVL 528
Cdd:smart00233   82 LQAESEEEREKWVEALRKAI 101
 
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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