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Conserved domains on  [gi|119855314|ref|YP_935917|]
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protein kinase [Mycobacterium sp. KMS]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
23-267 6.97e-45

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 158.94  E-value: 6.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  23 LGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDraFRERFVREADIASLLDHPGIVSIYGRGETDDgHLWIALQYVEGTD 102
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIKKEDSSS--LLEELLREIEILKKLNHPNIVKLYGVFEDEN-HLYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 103 AEAALQS--GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDEIGdgeRVFLTDFGVARPMDDTDRSMDGaF 180
Cdd:cd00180   78 LKDLLKEneGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNG---KVKLADFGLSKLLTSDKSLLKT-I 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 181 TATLAYSAPEVITGEQVDGR-SDIYSLGCTLFRLltgrqpfsqadgvvgtirahlampqprvsehvswatPELDQVIARA 259
Cdd:cd00180  154 VGTPAYMAPEVLLGKGYYSEkSDIWSLGVILYEL------------------------------------PELKDLIRKM 197

                 ....*...
gi 119855314 260 LAKDPAHR 267
Cdd:cd00180  198 LQKDPEKR 205
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
17-269 1.54e-63

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 210.85  E-value: 1.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314    17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSteLSRDRAFRERFVREADIASLLDHPGIVSIYGRGETDDgHLWIALQ 96
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDED-KLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314    97 YVEGTDAEAALQS-GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDeigDGeRVFLTDFGVARPMDDTDRS 175
Cdd:smart00220  78 YCEGGDLFDLLKKrGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DG-HVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   176 MDgaFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQADGVVGTIRaHLAMPQPRVSEHVSWATPELDQV 255
Cdd:smart00220 154 TT--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFK-KIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....
gi 119855314   256 IARALAKDPAHRFG 269
Cdd:smart00220 231 IRKLLVKDPEKRLT 244
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
23-267 6.97e-45

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 158.94  E-value: 6.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  23 LGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDraFRERFVREADIASLLDHPGIVSIYGRGETDDgHLWIALQYVEGTD 102
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIKKEDSSS--LLEELLREIEILKKLNHPNIVKLYGVFEDEN-HLYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 103 AEAALQS--GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDEIGdgeRVFLTDFGVARPMDDTDRSMDGaF 180
Cdd:cd00180   78 LKDLLKEneGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNG---KVKLADFGLSKLLTSDKSLLKT-I 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 181 TATLAYSAPEVITGEQVDGR-SDIYSLGCTLFRLltgrqpfsqadgvvgtirahlampqprvsehvswatPELDQVIARA 259
Cdd:cd00180  154 VGTPAYMAPEVLLGKGYYSEkSDIWSLGVILYEL------------------------------------PELKDLIRKM 197

                 ....*...
gi 119855314 260 LAKDPAHR 267
Cdd:cd00180  198 LQKDPEKR 205
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
55-177 8.84e-07

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine [Unknown function, General].


Pssm-ID: 234331  Cd Length: 199  Bit Score: 48.37  E-value: 8.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   55 DRAFR-ERFVREADIASLLDHPGIVS--IYgrgETDDGHLWIALQYVEGTDAEAALQSGAMtplravHIVTEVAKALDYA 131
Cdd:TIGR03724  36 DERIRrERTRNEARLLSRARKAGVNTpvVY---DVDPDNKTIVMEYIEGKPLKDVIEEGND------ELLREIGRLVGKL 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 119855314  132 HHRNVVHHDVKPANLLLSDeigdgERVFLTDFGVARPMDDT-DRSMD 177
Cdd:TIGR03724 107 HKAGIVHGDLTTSNIIVRD-----DKLYLIDFGLGKYSDEIeDKAVD 148
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
59-177 1.61e-06

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 47.66  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  59 RERFVREADIASLLDHPGIVS--IYgrgETDDGHLWIALQYVEGTDAEAALQSGAMTPLRAVHIvtEVAKAldyaHHRNV 136
Cdd:COG3642   43 RERTRREARILAKAREAGVPVpiVY---DVDPDNGLIVMEYIEGELLKDALEEARPDLLREVGR--LVGKL----HKAGI 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119855314 137 VHHDVKPANLLLSdeigdGERVFLTDFGVARPMDDT-DRSMD 177
Cdd:COG3642  114 VHGDLTTSNIILS-----GGRIYFIDFGLGEFSDEVeDKAVD 150
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
55-167 2.99e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 44.13  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  55 DRAFR-ERFVREADIASLLDHPGI--VSIYgrgETDDGHLWIALQYVEGTDAEAALQSGAMtplRAVHIVTEVAKALDYA 131
Cdd:PRK14879  38 DERIRrERTRREARIMSRARKAGVnvPAVY---FVDPENFIIVMEYIEGEPLKDLINSNGM---EELELSREIGRLVGKL 111
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119855314 132 HHRNVVHHDVKPANLLLSdeigdGERVFLTDFGVAR 167
Cdd:PRK14879 112 HSAGIIHGDLTTSNMILS-----GGKIYLIDFGLAE 142
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
17-210 1.46e-04

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 42.63  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVY---LAKNPTLPRRDALKVLSteLSRDRAFRERFVR----EADIASL------LDHPGIVSIYGR 83
Cdd:PHA02882  14 WKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIEN--LENETIVMETLVYnniyDIDKIALwknihnIDHLGIPKYYGC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  84 GETDDGHLW---IALQ-YVEGTDAEAALQSGAMTPLrAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLsdeigDGE-RV 158
Cdd:PHA02882  92 GSFKRCRMYyrfILLEkLVENTKEIFKRIKCKNKKL-IKNIMKDMLTTLEYIHEHGISHGDIKPENIMV-----DGNnRG 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 159 FLTDFGVA-------RPMDDTDRSMDgAFTATLAYSAPEVITGEQVDGRSDIYSLG-CTL 210
Cdd:PHA02882 166 YIIDYGIAshfiihgKHIEYSKEQKD-LHRGTLYYAGLDAHNGACVTRRGDLESLGyCML 224
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
123-222 4.75e-04

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 40.08  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   123 EVAKALDYAHHRNVVHHDVKPANLLLSdeiGDGERVFLTdfgvaRPMDDTDRsmdgaftatlAYSAPEVITGEQVDGRSD 202
Cdd:smart00750  25 QCLGALRELHRQAKSGNILLTWDGLLK---LDGSVAFKT-----PEQSRPDP----------YFMAPEVIQGQSYTEKAD 86
                           90       100
                   ....*....|....*....|
gi 119855314   203 IYSLGCTLFRLLTGRQPFSQ 222
Cdd:smart00750  87 IYSLGITLYEALDYELPYNE 106
YrbL-PhoP_reg pfam10707
PhoP regulatory network protein YrbL; This is a family of proteins that are activated by PhoP. ...
39-167 3.50e-03

PhoP regulatory network protein YrbL; This is a family of proteins that are activated by PhoP. PhoP protein controls the expression of a large number of genes that mediate adaptation to low Mg2+ environments and/or virulence in several bacterial species. YbrL is proposed to be acting in a loop activity with PhoP and PrmA analogous to the multicomponent loop in Salmonella where the PhoP-dependent PmrD protein activates the regulatory protein PmrA, and the activated PmrA then represses transcription from the PmrD promoter which harbours binding sites for both the PhoP and PmrA proteins. Expression of YrbL is induced in low Mg2+ in a PhoP-dependent fashion and repressed by Fe3+ in a PmrA-dependent manner.


Pssm-ID: 151200  Cd Length: 199  Bit Score: 37.62  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   39 LPRRDALKVLSTELSRDRAFRERfvreadiaSLLDHPGIVSIYGRGETD-------------DGHLWIALQYVegtdaea 105
Cdd:pfam10707  49 LLPTSRYRQNLRELKEYLRLSKR--------RGIDWSPIPRYYGFVETDlglglvterirdaDGNISPTLEDL------- 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119855314  106 aLQSGAMTPlravhivtEVAKALD------YAHHrnVVHHDVKPANLLLSDEIGDGERVFLTD-FGVAR 167
Cdd:pfam10707 114 -LKNGGLTA--------ALREALNefkrylLDNH--IVARDLNPHNIVYGRRSEGEYELVLVDgFGDPT 171
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
17-269 1.54e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 210.85  E-value: 1.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314    17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSteLSRDRAFRERFVREADIASLLDHPGIVSIYGRGETDDgHLWIALQ 96
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDED-KLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314    97 YVEGTDAEAALQS-GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDeigDGeRVFLTDFGVARPMDDTDRS 175
Cdd:smart00220  78 YCEGGDLFDLLKKrGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DG-HVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   176 MDgaFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQADGVVGTIRaHLAMPQPRVSEHVSWATPELDQV 255
Cdd:smart00220 154 TT--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFK-KIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|....
gi 119855314   256 IARALAKDPAHRFG 269
Cdd:smart00220 231 IRKLLVKDPEKRLT 244
Pkinase pfam00069
Protein kinase domain;
17-267 2.70e-54

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 186.30  E-value: 2.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSTElSRDRAFRERFVREADIASLLDHPGIVSIYGrGETDDGHLWIALQ 96
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLID-AFEDKDHLYLVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   97 YVEGTDAEAAL-QSGAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDEigdgERVFLTDFGVARPMDDTDRS 175
Cdd:pfam00069  79 YCEGGDLFDYLsRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDEN----GVVKIADFGLAKKLTKSSSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  176 MDGaFTATLAYSAPEVITGEQVDGR-SDIYSLGCTLFRLLTGRQPFSQaDGVVGTIRAHLAMPQPRVSEHVSWATPELD- 253
Cdd:pfam00069 155 LTT-FVGTPEYMAPEVLLGGNGYGPkVDVWSLGVILYELLTGKPPFSG-ESILDQLQLIRRILGPPLEFDEPKSDSGSEe 232
                         250
                  ....*....|....*.
gi 119855314  254 --QVIARALAKDPAHR 267
Cdd:pfam00069 233 akDLIKKCLNKDPSKR 248
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
16-270 2.27e-49

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 176.47  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  16 GYRIERVLGAGGMGTVYLAKNPtlpRRDALKVLSTELSRDRAFRERFVREADIASLLDHPG-IVSIYGRGEtDDGHLWIA 94
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQ-DEGSLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  95 LQYVEGTDAEAAL----QSGAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDeigDGERVFLTDFGVARPMD 170
Cdd:COG0515   77 MEYVDGGSLEDLLkkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDR---DGRVVKLIDFGLAKLLP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 171 D-----TDRSMDGAFTATLAYSAPEVITG---EQVDGRSDIYSLGCTLFRLLTGRQPF---SQADGVVGTIRAHLAMPQP 239
Cdd:COG0515  154 DpgstsSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILELPTP 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 119855314 240 RVSEHVSW-----ATPELDQVIARALAKDPAHRFGS 270
Cdd:COG0515  234 SLASPLSPsnpelISKAASDLLKKLLAKDPKNRLSS 269
pknD PRK13184
serine/threonine-protein kinase; Reviewed
17-270 9.23e-34

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 135.67  E-value: 9.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDRAFRERFVREADIASLLDHPGIVSIYGRgETDDGHLWIALQ 96
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSI-CSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  97 YVEGTDAEAALQS-----------------GAMTPlravhIVTEVAKALDYAHHRNVVHHDVKPANLLLsdeiGDGERVF 159
Cdd:PRK13184  83 YIEGYTLKSLLKSvwqkeslskelaektsvGAFLS-----IFHKICATIEYVHSKGVLHRDLKPDNILL----GLFGEVV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 160 LTDFGVARPMD-------DTDRSMD----------GAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQ 222
Cdd:PRK13184 154 ILDWGAAIFKKleeedllDIDVDERnicyssmtipGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRR 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 119855314 223 ADGVVGTIRAHLAMPQpRVSEHVSwATPELDQVIARALAKDPAHRFGS 270
Cdd:PRK13184 234 KKGRKISYRDVILSPI-EVAPYRE-IPPFLSQIAMKALAVDPAERYSS 279
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
44-267 8.33e-24

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 105.31  E-value: 8.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314    44 ALKVLSTELSRDRAFRERFVREADIASLLDHPGIVSIYGRGETDDGHLWIALQYVEGTDAEAALQS-GAMTPLRAVHIVT 122
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLREVLAAdGALPAGETGRLML 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314   123 EVAKALDYAHHRNVVHHDVKPANLLLSdEIGDGERVFLTDFGV------ARPMDDTDRSMDGAFTATLAYSAPEVITGEQ 196
Cdd:TIGR03903   87 QVLDALACAHNQGIVHRDLKPQNIMVS-QTGVRPHAKVLDFGIgtllpgVRDADVATLTRTTEVLGTPTYCAPEQLRGEP 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119855314   197 VDGRSDIYSLGCTLFRLLTGrQPFSQADGVVGTIRAHLAmPQPrVSEHVSWATPELDQVIARALAKDPAHR 267
Cdd:TIGR03903  166 VTPNSDLYAWGLIFLECLTG-QRVVQGASVAEILYQQLS-PVD-VSLPPWIAGHPLGQVLRKALNKDPRQR 233
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
18-268 1.26e-23

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 101.44  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  18 RIERVlGAGGMGTVYLAKNPTLPRRDALKVLSTelSRDRAFRERFVREADIASLLDHPGIVSIYGRGEtDDGHLWIALQY 97
Cdd:PLN00034  78 RVNRI-GSGAGGTVYKVIHRPTGRLYALKVIYG--NHEDTVRRQICREIEILRDVNHPNVVKCHDMFD-HNGEIQVLLEF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  98 VEGTDAEAA--LQSGAMTplravHIVTEVAKALDYAHHRNVVHHDVKPANLLlsdeIGDGERVFLTDFGVARPMDDTdrs 175
Cdd:PLN00034 154 MDGGSLEGThiADEQFLA-----DVARQILSGIAYLHRRHIVHRDIKPSNLL----INSAKNVKIADFGVSRILAQT--- 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 176 MD--GAFTATLAYSAPEVITGEQVDGR-----SDIYSLGCTLFRLLTGRQPFS---QADGvvGTIRAHLAMPQPrvSEHV 245
Cdd:PLN00034 222 MDpcNSSVGTIAYMSPERINTDLNHGAydgyaGDIWSLGVSILEFYLGRFPFGvgrQGDW--ASLMCAICMSQP--PEAP 297
                        250       260
                 ....*....|....*....|...
gi 119855314 246 SWATPELDQVIARALAKDPAHRF 268
Cdd:PLN00034 298 ATASREFRHFISCCLQREPAKRW 320
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
23-220 5.22e-20

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 90.26  E-value: 5.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  23 LGAGGMGTVYLAKNPTLPRRDALKVLST-ELSRDRAFrERFVREADIASLLDHPGIVSIYgRGETDDGHLWIALQYVEGT 101
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKrEILKMKQV-QHVAQEKSILMELSHPFIVNMM-CSFQDENRVYFLLEFVVGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 102 DAEAALQSGAMTPLR-AVHIVTEVAKALDYAHHRNVVHHDVKPANLLLsDEIGDgerVFLTDFGVARPMddTDRSmdgaF 180
Cdd:PTZ00263 104 ELFTHLRKAGRFPNDvAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL-DNKGH---VKVTDFGFAKKV--PDRT----F 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119855314 181 T--ATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPF 220
Cdd:PTZ00263 174 TlcGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
65-220 7.37e-15

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 73.74  E-value: 7.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  65 EADIASLL-DHPGIVSIYGRGETDDGHLWIaLQYVEGTDAEAALQS-GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVK 142
Cdd:PHA03390  58 EPMVHQLMkDNPNFIKLYYSVTTLKGHVLI-MDYIKDGDLFDLLKKeGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIK 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119855314 143 PANLLLSDEIgdgERVFLTDFGVARPMdDTDRSMDGaftaTLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPF 220
Cdd:PHA03390 137 LENVLYDRAK---DRIYLCDYGLCKII-GTPSCYDG----TLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF 206
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
296-386 1.84e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 296 RVGAAPD-TPGPRRTAPTPQASPPPATLKPLPPAPQQFGDADFRSAVKARRTPVKPPRADKAKREAPSTAARREPDFGGA 374
Cdd:PRK12323 376 TAAAAPVaQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA 455
                         90
                 ....*....|..
gi 119855314 375 AAPAPVVPRPAQ 386
Cdd:PRK12323 456 AAPAAAARPAAA 467
PHA03381 PHA03381
tegument protein VP22; Provisional
301-382 3.64e-05

tegument protein VP22; Provisional


Pssm-ID: 177618 [Multi-domain]  Cd Length: 290  Bit Score: 44.62  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 301 PDTPGPRRTAPTPQASPPPATLKPLPPAPqqfgdadfrSAVKARRTPVKPPRADKAKREAPSTAARREPDFGGAA---AP 377
Cdd:PHA03381  85 ADPRPSRRPHAQPEASGPGPARGARGPAG---------SRGRGRRAESPSPRDPPNPKGASAPRGRKSACADSAAlldAP 155

                 ....*
gi 119855314 378 APVVP 382
Cdd:PHA03381 156 APAAP 160
PLN03237 PLN03237
DNA topoisomerase 2; Provisional
296-395 8.22e-03

DNA topoisomerase 2; Provisional


Pssm-ID: 215641 [Multi-domain]  Cd Length: 1465  Bit Score: 37.92  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  296 RVGAAPDTP---GPRRTAPTPQASPPPATLKPLPPAPQQFGDADFRSAVKARRT----PVKPPRADKAK---REAPSTAA 365
Cdd:PLN03237 1323 EVSLAERLKkkgGRKPAAANKKAAKPPAAAKKRGPATVQSGQKLLTEMLKPAEAigisPEKKVRKMRASpfnKKSGSVLG 1402
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 119855314  366 R---------REPDFGGAA-----APAPVVPRPAQRREVPKHVV 395
Cdd:PLN03237 1403 RaatnketesSENVSGSSSsekdeIDVSAKPRPQRANRKQTTYV 1446
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
23-267 6.97e-45

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 158.94  E-value: 6.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  23 LGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDraFRERFVREADIASLLDHPGIVSIYGRGETDDgHLWIALQYVEGTD 102
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIKKEDSSS--LLEELLREIEILKKLNHPNIVKLYGVFEDEN-HLYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 103 AEAALQS--GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDEIGdgeRVFLTDFGVARPMDDTDRSMDGaF 180
Cdd:cd00180   78 LKDLLKEneGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNG---KVKLADFGLSKLLTSDKSLLKT-I 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 181 TATLAYSAPEVITGEQVDGR-SDIYSLGCTLFRLltgrqpfsqadgvvgtirahlampqprvsehvswatPELDQVIARA 259
Cdd:cd00180  154 VGTPAYMAPEVLLGKGYYSEkSDIWSLGVILYEL------------------------------------PELKDLIRKM 197

                 ....*...
gi 119855314 260 LAKDPAHR 267
Cdd:cd00180  198 LQKDPEKR 205
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
17-267 5.91e-42

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 151.59  E-value: 5.91e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDRafrERFVREADIASLLDHPGIVSIYGrGETDDGHLWIALQ 96
Cdd:cd05122    2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKK---EKIINEIQILKKCKHPNIVKYYG-SYLKKDELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  97 YVEGTDAEAALQSgAMTPLRAVHIVT---EVAKALDYAHHRNVVHHDVKPANLLLSDeigDGErVFLTDFGVARPMDDTD 173
Cdd:cd05122   78 FCSGGSLKDLLKS-TNQTLTESQIAYvckELLKGLEYLHSNGIIHRDIKAANILLTS---DGE-VKLIDFGLSAQLSDTK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 174 RSMdgAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQadgvVGTIRA--HLAMPQPRVSEHVSWATPE 251
Cdd:cd05122  153 ARN--TMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSE----LPPMKAlfKIATNGPPGLRNPEKWSDE 226
                        250
                 ....*....|....*.
gi 119855314 252 LDQVIARALAKDPAHR 267
Cdd:cd05122  227 FKDFLKKCLQKNPEKR 242
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
17-267 8.68e-42

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 151.50  E-value: 8.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNptlpRRD----ALKVLSTELSRDRAfRERFVREADIASLLDHPGIVSIYGRGEtDDGHLW 92
Cdd:cd08215    2 YEIIKQIGKGSFGKVYLVRR----KSDgklyVLKEIDLSNMSEKE-REDALNEVKILKKLNHPNIIKYYESFE-EKGKLC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  93 IALQYVEGTDAEAALQSGAM--TPLR---AVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDeigDGeRVFLTDFGVAR 167
Cdd:cd08215   76 IVMEYADGGDLSQKIKKQKKegKPFPeeqILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTS---NG-LVKLGDFGISK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 168 PMDDTDrSMDGAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFsQADGVVGTIRAHLAMPQPRVSEHVSw 247
Cdd:cd08215  152 VLSSTV-DLAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPF-EGENLLELALKILKGQYPPIPSQYS- 228
                        250       260
                 ....*....|....*....|
gi 119855314 248 atPELDQVIARALAKDPAHR 267
Cdd:cd08215  229 --SELRNLVSSLLQKDPEER 246
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
17-267 3.36e-40

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK 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. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 146.93  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLstELSRDRAFR-ERFVREADIASLLDHPGIVSIYG-RGETDDGHLWIA 94
Cdd:cd06606    2 WTRGELLGRGSFGSVYLALDKDTGELMAVKSV--ELSGDSEEElEALEREIRILSSLQHPNIVRYYGsERDEEKNTLNIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  95 LQYVEGTDAEAALQS-GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSdeiGDGeRVFLTDFGVARPMDDTD 173
Cdd:cd06606   80 LEYVSGGSLSSLLKKfGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVD---SDG-VVKLADFGCAKRLGDIE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 174 -RSMDGAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQADGVVGTIrAHLAMPQ--PRVSEHVSwatP 250
Cdd:cd06606  156 tGEGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSELGNPMAAL-YKIGSSGepPEIPEHLS---E 231
                        250
                 ....*....|....*..
gi 119855314 251 ELDQVIARALAKDPAHR 267
Cdd:cd06606  232 EAKDFLRKCLRRDPKKR 248
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
23-270 4.13e-35

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 132.26  E-value: 4.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  23 LGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDRAFRERFVREADIASLLDHPGIVSIYgRGETDDGHLWIALQYVEGTD 102
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLKKKKIIKRKEVEHTLTERNILSRINHPFIVKLH-YAFQTEEKLYLVLEYAPGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 103 AEAALQS-GAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDeigDGErVFLTDFGVARPMDDTDRSMDGaFT 181
Cdd:cd05123   80 LFSHLSKeGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDA---DGH-IKLTDFGLAKELSSEGSRTNT-FC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 182 ATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFsQADGVVGTIRAHLAMPqPRVSEHVSwatPELDQVIARALA 261
Cdd:cd05123  155 GTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF-YAEDRKEIYEKILKDP-LRFPEFLS---PEARDLISGLLQ 229

                 ....*....
gi 119855314 262 KDPAHRFGS 270
Cdd:cd05123  230 KDPTKRLGS 238
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
18-267 9.03e-34

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 128.86  E-value: 9.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  18 RIERVLGAGGMGTVYLAKNPTLPRRDALKVLSteLSRDRAFRERFVREADIASLLDHPGIVSIYGRGEtDDGHLWIALQY 97
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFY-KEGEISIVLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  98 VE-GTDAEAALQSGAMTPLRAVHIVTEVAKALDYAHH-RNVVHHDVKPANLLLSDeigDGErVFLTDFGVARPMDDTdrs 175
Cdd:cd06623   81 MDgGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINS---KGE-VKIADFGISKVLENT--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 176 MDGAFTA--TLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQAD-GVVGTIRAHLAM-PQPRVSEHVswATPE 251
Cdd:cd06623  154 LDQCNTFvgTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGqPSFFELMQAICDgPPPSLPAEE--FSPE 231
                        250
                 ....*....|....*.
gi 119855314 252 LDQVIARALAKDPAHR 267
Cdd:cd06623  232 FRDFISACLQKDPKKR 247
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
17-267 1.74e-32

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3-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. 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.


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 125.42  E-value: 1.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDRAfrERFVREADIASLLDHPGIVSIYGrGETDDGHLWIALQ 96
Cdd:cd06609    3 FTLLECIGKGSFGEVYKAIDKRTNQVVAIKVIDLEEAEDEI--EDIQQEIQFLSQCRSPYITKYYG-SFLKGSKLWIIME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  97 YVEGTDAEAALQSGAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDEiGDgerVFLTDFGVARPMDDTDRSM 176
Cdd:cd06609   80 YCGGGSCLDLLKPGKLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANILLSEE-GD---VKLADFGVSGQLTSTMSKR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 177 DgAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQADgvvgTIRAHLAMPQ--PRVSEHVSWaTPELDQ 254
Cdd:cd06609  156 N-TFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLH----PMRVLFLIPKnnPPSLEGNKF-SKPFKD 229
                        250
                 ....*....|...
gi 119855314 255 VIARALAKDPAHR 267
Cdd:cd06609  230 FVSLCLNKDPKER 242
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
23-267 3.91e-32

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 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. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 124.37  E-value: 3.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  23 LGAGGMGTVYLAKNPTLPRRDALKVLSTELSRDRAFRErFVREADIASLLDHPGIVSIYGRgETDDGHLWIALQYVEGTD 102
Cdd:cd06626    8 IGGGTFGKVYTAVNLDTGELMAVKEIRIQDNDPKTIKE-IADEMKVLELLKHPNLVKYYGV-EVHREKVYIFMEYCSGGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 103 AEAALQSGAMTPLRAVHIVT-EVAKALDYAHHRNVVHHDVKPANLLLsdeiGDGERVFLTDFGVARPMDDTDRSMDGAF- 180
Cdd:cd06626   86 LEELLEHGRILDEHVIRVYTlQLLEGLAYLHSHGIVHRDIKPANIFL----DHNGVIKLGDFGCAVKLKNNTTTMGEEVq 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 181 --TATLAYSAPEVITGEQVDGR---SDIYSLGCTLFRLLTGRQPFSQADGVVgTIRAHLAMPQPRVSEHVSWATPELDQV 255
Cdd:cd06626  162 slAGTPAYMAPEVITGGKGKGHgraADIWSLGCVVLEMATGKRPWSELDNEF-QIMFHVGAGHKPPIPDSLQLSPEGKDF 240
                        250
                 ....*....|..
gi 119855314 256 IARALAKDPAHR 267
Cdd:cd06626  241 LDRCLESDPKKR 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
21-267 1.47e-31

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. 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.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 122.81  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  21 RVLGAGGMGTVYLAKNPTLPRRDALKVLSTELsrDRAFRERFVREADIASLLDHPGIVSIYGrGETDDGHLWIALQYVEG 100
Cdd:cd06605    7 GELGAGNSGVVSKVLHRPTGKIMAVKTIRLEI--NEAIQKQILRELDILHKCNSPYIVGFYG-AFYNNGDISICMEYMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 101 TDAEAALQSGA-MTPLRAV-HIVTEVAKALDYAHH-RNVVHHDVKPANLLLSDEigdGErVFLTDFGVARPMDDtdrSMD 177
Cdd:cd06605   84 GSLDKILKEVQgRIPERILgKIAVAVLKGLTYLHEkHKIIHRDVKPSNILVNSR---GQ-IKLCDFGVSGQLVN---SLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314 178 GAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQADGVVGTIRAHLA----MPQPRVSEHVswATPELD 253
Cdd:cd06605  157 KTFVGTSSYMAPERIQGNDYSVKSDIWSLGLSLIELATGRFPYPPENDPPDGIFELLQyivnEPPPRLPSGK--FSPDFQ 234
                        250
                 ....*....|....
gi 119855314 254 QVIARALAKDPAHR 267
Cdd:cd06605  235 DFVNLCLIKDPRER 248
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
17-222 4.47e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 118.83  E-value: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSTE-LSRDRafRERFV-READIASLLD-HPGIVSIYGrgeT--DDGHL 91
Cdd:cd05581    3 FKFGKIIGEGSFSTVVLAKEKETNKEYAIKILDKRqLIKEK--KVKYVkIEKEVLTRLNgHPGIIKLYY---TfqDEENL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  92 WIALQYVEGTD-AEAALQSGAMTPLRAVHIVTEVAKALDYAHHRNVVHHDVKPANLLLSDeigDGeRVFLTDFGVARPMD 170
Cdd:cd05581   78 YFVLEYAPNGElLQYIRKYGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDK---DM-HIKITDFGTAKVLD 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119855314 171 DTD-------------------RSMDGAFTATLAYSAPEVITGEQVDGRSDIYSLGCTLFRLLTGRQPFSQ 222
Cdd:cd05581  154 PNSspesnkgdatnidsqieknRRRFASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRG 224
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
17-220 6.27e-30

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. 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. 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.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 117.73  E-value: 6.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119855314  17 YRIERVLGAGGMGTVYLAKNPTLPRRDALKVLSTElSRDRAFRERFVREADIASLLDHPGIVSIYGRGETDDgHLWIALQ 96
Cdd:cd06627