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Conserved domains on  [gi|72163465|ref|YP_291122|]
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serine/threonine protein kinase [Thermobifida fusca YX]

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List of domain hits

Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
428-488 1.48e-17

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


:

Pssm-ID: 119328  Cd Length: 62  Bit Score: 77.57  E-value: 1.48e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72163465 428 EMPDLVGMSQADALGEINRAGLARGEITHQESDE-PQGTVLSTDPKAGTEVEPGTKVNLVVA 488
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDvPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
495-553 2.84e-17

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


:

Pssm-ID: 119328  Cd Length: 62  Bit Score: 76.80  E-value: 2.84e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 495 EVPSLAGMNEDQARERLAELGLTLEAQTQETSDATP-GTAIAQSPQAGTKVERGTTVTVT 553
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPkGTVISQSPAAGTKVKKGSTVTLT 60
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
358-421 1.14e-15

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


:

Pssm-ID: 119328  Cd Length: 62  Bit Score: 72.18  E-value: 1.14e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72163465 358 TIPNVAGMSVEEATETLQEKGFENIEVADEPtpSNEIEEGKVVGTDPEIGETVPPDTEITILIS 421
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEY--SDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-267 6.72e-48

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: 168.83  E-value: 6.72e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  10 RYQLEAPVGRGGMAEVFRARDLRLDRLVAVKtlRSDLAR-DPTFQARFRREAQSAASLNHPSIIAVYdtgEDVIDGVPIp 88
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLK--EIDLSNmSEKEREDALNEVKILKKLNHPNIIKYY---ESFEEKGKL- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  89 YIVMEYVDGRTLKELLED---NRRLLPERT-LEITDGILRALAAAHARGIVHRDIKPANVMLTRQAEVKVMDFGIARAMN 164
Cdd:cd08215  75 CIVMEYADGGDLSQKIKKqkkEGKPFPEEQiLDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 165 DAQAtMTQTsqVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVREEPIP-PTELDPEi 243
Cdd:cd08215 155 STVD-LAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPiPSQYSSE- 230
                       250       260
                ....*....|....*....|....
gi 72163465 244 pewIEAIVLRAMAKDREQRYQTAE 267
Cdd:cd08215 231 ---LRNLVSSLLQKDPEERPSIAQ 251
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-272 3.85e-65

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 215.47  E-value: 3.85e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465     11 YQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRsdLARDPTFQARFRREAQSAASLNHPSIIAVYDTGEDVIDgvpiPYI 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK----LYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465     91 VMEYVDGRTLKELLEDNRRLLPER----TLEITDGILRALAAaharGIVHRDIKPANVMLTRQAEVKVMDFGIARAMNDA 166
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEarfyLRQILSALEYLHSK----GIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    167 QATMTqtsqVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVREEPIPPTELDPEIPEw 246
Cdd:smart00220 151 EKLTT----FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISP- 225
                          250       260
                   ....*....|....*....|....*...
gi 72163465    247 iEAI--VLRAMAKDREQRYqTAEEMRAD 272
Cdd:smart00220 226 -EAKdlIRKLLVKDPEKRL-TAEEALQH 251
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
328-556 5.34e-53

Uncharacterized protein conserved in bacteria [Function unknown]


:

Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 184.54  E-value: 5.34e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 328 KVLWVLLGTAVLAAAAFLgwllFNPgtDNITIPNVAGMSVEEATETLQEKGFEnIEVADEPtpSNEIEEGKVVGTDPEIG 407
Cdd:COG2815   3 SLLVSLVVAGVLLATFFP----VSP--DKVKVPNVAGLDEEDAKAELQKAGLE-VGVRERE--SDKVPEGKVIRTDPKAG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 408 ETVPPDTEITILISGGPEMIEMPDLVGMSQADALGEINRAGLARGEITHQE--SDEPQGTVLSTDPKAGTEVEPGTKVNL 485
Cdd:COG2815  74 TVVKQGSKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKITQEEvsDEVPAGTVISQSPSAGTEVKPGETVKL 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72163465 486 VVAKASTKVEVPSLAGMNEDQARERLAELGLTLEAQTQETSDATPGTAIAQSPQAGTKVERGTTVTVTFAK 556
Cdd:COG2815 154 TVSKGPETITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSK 224
 
Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
428-488 1.48e-17

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 77.57  E-value: 1.48e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72163465 428 EMPDLVGMSQADALGEINRAGLARGEITHQESDE-PQGTVLSTDPKAGTEVEPGTKVNLVVA 488
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDvPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
495-553 2.84e-17

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 76.80  E-value: 2.84e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 495 EVPSLAGMNEDQARERLAELGLTLEAQTQETSDATP-GTAIAQSPQAGTKVERGTTVTVT 553
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPkGTVISQSPAAGTKVKKGSTVTLT 60
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
358-421 1.14e-15

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 72.18  E-value: 1.14e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72163465 358 TIPNVAGMSVEEATETLQEKGFENIEVADEPtpSNEIEEGKVVGTDPEIGETVPPDTEITILIS 421
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEY--SDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-267 6.72e-48

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: 168.83  E-value: 6.72e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  10 RYQLEAPVGRGGMAEVFRARDLRLDRLVAVKtlRSDLAR-DPTFQARFRREAQSAASLNHPSIIAVYdtgEDVIDGVPIp 88
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLK--EIDLSNmSEKEREDALNEVKILKKLNHPNIIKYY---ESFEEKGKL- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  89 YIVMEYVDGRTLKELLED---NRRLLPERT-LEITDGILRALAAAHARGIVHRDIKPANVMLTRQAEVKVMDFGIARAMN 164
Cdd:cd08215  75 CIVMEYADGGDLSQKIKKqkkEGKPFPEEQiLDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 165 DAQAtMTQTsqVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVREEPIP-PTELDPEi 243
Cdd:cd08215 155 STVD-LAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPiPSQYSSE- 230
                       250       260
                ....*....|....*....|....
gi 72163465 244 pewIEAIVLRAMAKDREQRYQTAE 267
Cdd:cd08215 231 ---LRNLVSSLLQKDPEERPSIAQ 251
PASTA smart00740
PASTA domain;
423-489 2.59e-16

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 74.26  E-value: 2.59e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72163465    423 GPEMIEMPDLVGMSQADALGEINRAGLARGEITHQESDEPQGTVLSTDPKAGTEVEPGTKVNLVVAK 489
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
427-489 3.77e-16

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 252166  Cd Length: 63  Bit Score: 73.80  E-value: 3.77e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 72163465   427 IEMPDLVGMSQADALGEINRAGLARGEITHQESDEPQGTVLSTDPKAGTEVEPGTKVNLVVAK 489
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
494-556 7.10e-16

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 252166  Cd Length: 63  Bit Score: 73.03  E-value: 7.10e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 72163465   494 VEVPSLAGMNEDQARERLAELGLTLEAQTQETSDATPGTAIAQSPQAGTKVERGTTVTVTFAK 556
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
491-556 4.44e-15

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 70.80  E-value: 4.44e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 72163465    491 STKVEVPSLAGMNEDQARERLAELGLTLEAQTQETSDATPGTAIAQSPQAGTKVERGTTVTVTFAK 556
Cdd:smart00740   2 PEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA smart00740
PASTA domain;
353-422 5.37e-14

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 67.72  E-value: 5.37e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    353 GTDNITIPNVAGMSVEEATETLQEKGFEnieVADEPTPSNEIEEGKVVGTDPEIGETVPPDTEITILISG 422
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLK---VEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
357-422 8.96e-14

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 252166  Cd Length: 63  Bit Score: 66.87  E-value: 8.96e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 72163465   357 ITIPNVAGMSVEEATETLQEKGFEnieVADEPTPSNEIEEGKVVGTDPEIGETVPPDTEITILISG 422
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLK---VGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
16-168 6.08e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 61.08  E-value: 6.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   16 PVGRGGMAEVFRARDLRLDrlVAVKTLRSDLARDPTFQARFRR-----EAQ-----SAASLNHPSIIAVydtgeDVIDGV 85
Cdd:PRK14879   3 LIKRGAEAEIYLGDFLGIK--AVIKWRIPKRYRHPELDERIRRertrrEARimsraRKAGVNVPAVYFV-----DPENFI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   86 pipyIVMEYVDGRTLKELLEDNRRLLPERTLEItdGIlrALAAAHARGIVHRDIKPANVMLtRQAEVKVMDFGIARAMND 165
Cdd:PRK14879  76 ----IVMEYIEGEPLKDLINSNGMEELELSREI--GR--LVGKLHSAGIIHGDLTTSNMIL-SGGKIYLIDFGLAEFSKD 146

                 ...
gi 72163465  166 AQA 168
Cdd:PRK14879 147 LED 149
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
14-161 1.72e-06

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 47.66  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  14 EAPVGRGGMAEVFRarDLRLDRLVAVKTLRSDLARDPTFQARFRREAqsaaSLNHPSIIA-VYDTGedvidgVPIPY--- 89
Cdd:COG3642   1 MDLIKQGAEAIIYL--TDFLGLPAVVKERIPKRYRHPELDEKLRRER----TRREARILAkAREAG------VPVPIvyd 68
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72163465  90 -------IVMEYVDGRTLKELLEDNRRLLPERtleitdgILRALAAAHARGIVHRDIKPANVMLTRQaEVKVMDFGIAR 161
Cdd:COG3642  69 vdpdnglIVMEYIEGELLKDALEEARPDLLRE-------VGRLVGKLHKAGIVHGDLTTSNIILSGG-RIYFIDFGLGE 139
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
17-161 1.95e-06

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: 47.60  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    17 VGRGGMAEVFRARdlRLDRLVAVKTLRSDLARDPTFQARFRRE-AQSAASLnhpsIIAVYDTGedVIdgVPIPY------ 89
Cdd:TIGR03724   2 IAKGAEAIIYLGD--FLGLKAVIKERVPKSYRHPELDERIRRErTRNEARL----LSRARKAG--VN--TPVVYdvdpdn 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72163465    90 --IVMEYVDGRTLKELLEDNRrllpertLEITDGILRALAAAHARGIVHRDIKPANVMLtRQAEVKVMDFGIAR 161
Cdd:TIGR03724  72 ktIVMEYIEGKPLKDVIEEGN-------DELLREIGRLVGKLHKAGIVHGDLTTSNIIV-RDDKLYLIDFGLGK 137
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
133-206 5.97e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 37.62  E-value: 5.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72163465  133 GIVHRDIKPANVMLTRQAEVKVMDFGIAR--AMNDAQATMTQTSQVI--GTAQYLSPEQARGERVDVRSDIYSTG-CVL 206
Cdd:PHA02882 146 GISHGDIKPENIMVDGNNRGYIIDYGIAShfIIHGKHIEYSKEQKDLhrGTLYYAGLDAHNGACVTRRGDLESLGyCML 224
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-272 3.85e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 215.47  E-value: 3.85e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465     11 YQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRsdLARDPTFQARFRREAQSAASLNHPSIIAVYDTGEDVIDgvpiPYI 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDK----LYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465     91 VMEYVDGRTLKELLEDNRRLLPER----TLEITDGILRALAAaharGIVHRDIKPANVMLTRQAEVKVMDFGIARAMNDA 166
Cdd:smart00220  75 VMEYCEGGDLFDLLKKRGRLSEDEarfyLRQILSALEYLHSK----GIVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    167 QATMTqtsqVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVREEPIPPTELDPEIPEw 246
Cdd:smart00220 151 EKLTT----FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISP- 225
                          250       260
                   ....*....|....*....|....*...
gi 72163465    247 iEAI--VLRAMAKDREQRYqTAEEMRAD 272
Cdd:smart00220 226 -EAKdlIRKLLVKDPEKRL-TAEEALQH 251
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
328-556 5.34e-53

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 184.54  E-value: 5.34e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 328 KVLWVLLGTAVLAAAAFLgwllFNPgtDNITIPNVAGMSVEEATETLQEKGFEnIEVADEPtpSNEIEEGKVVGTDPEIG 407
Cdd:COG2815   3 SLLVSLVVAGVLLATFFP----VSP--DKVKVPNVAGLDEEDAKAELQKAGLE-VGVRERE--SDKVPEGKVIRTDPKAG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 408 ETVPPDTEITILISGGPEMIEMPDLVGMSQADALGEINRAGLARGEITHQE--SDEPQGTVLSTDPKAGTEVEPGTKVNL 485
Cdd:COG2815  74 TVVKQGSKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLNLSKITQEEvsDEVPAGTVISQSPSAGTEVKPGETVKL 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72163465 486 VVAKASTKVEVPSLAGMNEDQARERLAELGLTLEAQTQETSDATPGTAIAQSPQAGTKVERGTTVTVTFAK 556
Cdd:COG2815 154 TVSKGPETITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSK 224
pknD PRK13184
serine/threonine-protein kinase; Reviewed
9-293 1.16e-52

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 193.45  E-value: 1.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    9 GRYQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRSDLARDPTFQARFRREAQSAASLNHPSIIAVYdTGEDviDGVPIp 88
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVY-SICS--DGDPV- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   89 YIVMEYVDGRTLKELLEDNRRL------LPERT-----LEITDGILRALAAAHARGIVHRDIKPANVMLTRQAEVKVMDF 157
Cdd:PRK13184  78 YYTMPYIEGYTLKSLLKSVWQKeslskeLAEKTsvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  158 GIARAMNDAQ---------------ATMTQTSQVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPV 222
Cdd:PRK13184 158 GAAIFKKLEEedlldidvdernicySSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGR 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 72163465  223 SIAYQHVREepiPPTELDP--EIPEWIEAIVLRAMAKDREQRYQTAEEMRADIQRGLQGMPTAASTMALSAAN 293
Cdd:PRK13184 238 KISYRDVIL---SPIEVAPyrEIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSPEWTVKATLMTKK 307
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
11-275 1.84e-52

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: 185.33  E-value: 1.84e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  11 YQLEAPVGRGGMAEVFRARDLRLdrlVAVKTLRSDLARDPTFQARFRREAQSAASLNHPS-IIAVYDTGEDviDGvpIPY 89
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQD--EG--SLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  90 IVMEYVDGRTLKELLEDNRR---LLPERTLEITDGILRALAAAHARGIVHRDIKPANVMLTRQ-AEVKVMDFGIARAMND 165
Cdd:COG0515  75 LVMEYVDGGSLEDLLKKIGRkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 166 AQATMTQ---TSQVIGTAQYLSPEQARG---ERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSI---AYQHVREEPIP- 235
Cdd:COG0515 155 PGSTSSIpalPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSAtsqTLKIILELPTPs 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 72163465 236 -----PTELDPEIPEWIEAIVLRAMAKDREQRYQTAEEMRADIQR 275
Cdd:COG0515 235 lasplSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA 279
Pkinase pfam00069
Protein kinase domain;
11-268 1.44e-47

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 168.19  E-value: 1.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    11 YQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRSDLaRDPTFQARFRREAQSAASLNHPSIIAVYDTGEDviDGVPipYI 90
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRS-EKSKKDQTARREIRILRRLSHPNIVRLIDAFED--KDHL--YL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    91 VMEYVDGRTLKELLEDNRRLlPERT-----LEITDGILRALAAaharGIVHRDIKPANVMLTRQAEVKVMDFGIARAMND 165
Cdd:pfam00069  76 VMEYCEGGDLFDYLSRGGPL-SEDEakkiaLQILRGLEYLHSN----GIIHRDLKPENILLDENGVVKIADFGLAKKLTK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   166 AQATMTqtsQVIGTAQYLSPEQARGER-VDVRSDIYSTGCVLYELLTGRPPFVGDSPVSiAYQHVREEPIPPTELD---- 240
Cdd:pfam00069 151 SSSSLT---TFVGTPEYMAPEVLLGGNgYGPKVDVWSLGVILYELLTGKPPFSGESILD-QLQLIRRILGPPLEFDepks 226
                         250       260
                  ....*....|....*....|....*...
gi 72163465   241 PEIPEWIEAIVLRAMAKDREQRYqTAEE 268
Cdd:pfam00069 227 DSGSEEAKDLIKKCLNKDPSKRP-TAEE 253
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-269 1.91e-36

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: 144.99  E-value: 1.91e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465     37 VAVKTLRSDLARDPTFQARFRREAQSAASLNHPSIIAVYDTGEDVIDGVpipYIVMEYVDGRTLKELLEDNRRLLPERTL 116
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLL---FAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    117 EITDGILRALAAAHARGIVHRDIKPANVMLTR---QAEVKVMDFGIARAMNDAQ----ATMTQTSQVIGTAQYLSPEQAR 189
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQtgvRPHAKVLDFGIGTLLPGVRdadvATLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465    190 GERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVREEPIppteldpEIPEWIEAI----VLR-AMAKDREQRYQ 264
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDV-------SLPPWIAGHplgqVLRkALNKDPRQRAA 235

                   ....*
gi 72163465    265 TAEEM 269
Cdd:TIGR03903  236 SAPAL 240
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
10-219 1.13e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.13  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   10 RY-QLEAPVGRGGMAEVFRARDLRLDRLVAVKTLR-SDLARDPTFQARF----------RREAQSAASLNHPSIIAVYD- 76
Cdd:PTZ00024   9 RYiQKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKiIEISNDVTKDRQLvgmcgihfttLRELKIMNEIKHENIMGLVDv 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   77 -TGEDVIDgvpipyIVMEYVDGrTLKELLEDNRRLLPERTLEITDGILRALAAAHARGIVHRDIKPANVMLTRQAEVKVM 155
Cdd:PTZ00024  89 yVEGDFIN------LVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72163465  156 DFGIARA------------MNDAQATMTQTSQVIgTAQYLSPEQARG-ERVDVRSDIYSTGCVLYELLTGRPPFVGD 219
Cdd:PTZ00024 162 DFGLARRygyppysdtlskDETMQRREEMTSKVV-TLWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKPLFPGE 237
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
10-222 2.20e-15

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 75.62  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   10 RYQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRSDlARDPTFQARFRREAQSAASLNHPSIIAVYDtgedVIDGVPIPY 89
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLE-QEDEGVPSTAIREISLLKEMQHGNIVRLQD----VVHSEKRLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   90 IVMEYVDGRTLKEL-----LEDNRRLLPERTLEITDGILRALAAAhargIVHRDIKPANVMLTRQAE-VKVMDFGIARAM 163
Cdd:PLN00009  78 LVFEYLDLDLKKHMdsspdFAKNPRLIKTYLYQILRGIAYCHSHR----VLHRDLKPQNLLIDRRTNaLKLADFGLARAF 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  164 NDAQATMTQtsQVIgTAQYLSPEQARGER-VDVRSDIYSTGCVLYELLTGRPPFVGDSPV 222
Cdd:PLN00009 154 GIPVRTFTH--EVV-TLWYRAPEILLGSRhYSTPVDIWSVGCIFAEMVNQKPLFPGDSEI 210
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
89-219 4.29e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 62.57  E-value: 4.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   89 YIVMEYVDGRTLKELLEDNRRLlPERT-----LEITDGILRALAAAhargIVHRDIKPANVMLTR-QAEVKVMDFGIARA 162
Cdd:PHA03390  85 VLIMDYIKDGDLFDLLKKEGKL-SEAEvkkiiRQLVEALNDLHKHN----IIHNDIKLENVLYDRaKDRIYLCDYGLCKI 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 72163465  163 MNdaqatmtQTSQVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGD 219
Cdd:PHA03390 160 IG-------TPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKED 209
spoVD_pbp TIGR02214
stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the ...
365-555 7.83e-05

stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the cell division protein FtsI, a penicillin binding protein. This subfamily is restricted to Bacillus subtilis and related Gram-positive species with known or suspected endospore formation capability. In these species, the functional equivalent of FtsI is desginated PBP-2B, a paralog of spoVD [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination].


Pssm-ID: 131269 [Multi-domain]  Cd Length: 636  Bit Score: 44.03  E-value: 7.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   365 MSVEEATETLQEKG------FENIEV------ADEPTPSNEIEEGKVVGTdpEIGETVPPDTEITILISggpemIEMPDL 432
Cdd:TIGR02214 462 QKLRLALETVVSKGsgknafIEGYRVggktgtAQKVKPNGGYMEGEYIVS--FVGFAPADDPAVAVLVV-----VDNPKG 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   433 V----GMSQADALGEINRAGLargeithqesdepqgTVLSTDPKAGTEVEPGTKVNLVVAkastkVEVPSLAGMNEDQAR 508
Cdd:TIGR02214 535 VqqfgGLVAAPVFGSVFNDIL---------------NYLGIKPQMNQGEAPAAATNQVEA-----VAVPNLRGMKVDDAE 594
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 72163465   509 ERLAELGLTLEAQTQETSdatpgtAIAQSPQAGTKVERGTTVTVTFA 555
Cdd:TIGR02214 595 KTLLHLGLDVATEGFGTR------VVNQTPIPGEKVKEGTKVVLYLG 635
 
Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
428-488 1.48e-17

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 77.57  E-value: 1.48e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72163465 428 EMPDLVGMSQADALGEINRAGLARGEITHQESDE-PQGTVLSTDPKAGTEVEPGTKVNLVVA 488
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDvPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
495-553 2.84e-17

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 76.80  E-value: 2.84e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 495 EVPSLAGMNEDQARERLAELGLTLEAQTQETSDATP-GTAIAQSPQAGTKVERGTTVTVT 553
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPkGTVISQSPAAGTKVKKGSTVTLT 60
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
358-421 1.14e-15

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 72.18  E-value: 1.14e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72163465 358 TIPNVAGMSVEEATETLQEKGFENIEVADEPtpSNEIEEGKVVGTDPEIGETVPPDTEITILIS 421
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEY--SDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-267 6.72e-48

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: 168.83  E-value: 6.72e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  10 RYQLEAPVGRGGMAEVFRARDLRLDRLVAVKtlRSDLAR-DPTFQARFRREAQSAASLNHPSIIAVYdtgEDVIDGVPIp 88
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLK--EIDLSNmSEKEREDALNEVKILKKLNHPNIIKYY---ESFEEKGKL- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  89 YIVMEYVDGRTLKELLED---NRRLLPERT-LEITDGILRALAAAHARGIVHRDIKPANVMLTRQAEVKVMDFGIARAMN 164
Cdd:cd08215  75 CIVMEYADGGDLSQKIKKqkkEGKPFPEEQiLDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 165 DAQAtMTQTsqVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVREEPIP-PTELDPEi 243
Cdd:cd08215 155 STVD-LAKT--VVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPiPSQYSSE- 230
                       250       260
                ....*....|....*....|....
gi 72163465 244 pewIEAIVLRAMAKDREQRYQTAE 267
Cdd:cd08215 231 ---LRNLVSSLLQKDPEERPSIAQ 251
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
10-268 4.33e-43

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: 155.41  E-value: 4.33e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  10 RYQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRsdLARDPTFQAR-FRREAQSAASLNHPSIIAVYDTGEDVIDGVPip 88
Cdd:cd06606   1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSVE--LSGDSEEELEaLEREIRILSSLQHPNIVRYYGSERDEEKNTL-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  89 YIVMEYVDGRTLKELLEDNRRLlPER-----TLEITDGILRALAAaharGIVHRDIKPANVMLTRQAEVKVMDFGIARAM 163
Cdd:cd06606  77 NIFLEYVSGGSLSSLLKKFGKL-PEPvirkyTRQILEGLAYLHSN----GIVHRDIKGANILVDSDGVVKLADFGCAKRL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 164 NDAqATMTQTSQVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVG-DSPVSIAYQhvreepIPPTELDPE 242
Cdd:cd06606 152 GDI-ETGEGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSElGNPMAALYK------IGSSGEPPE 224
                       250       260       270
                ....*....|....*....|....*....|
gi 72163465 243 IPEWI--EAI--VLRAMAKDREQRYqTAEE 268
Cdd:cd06606 225 IPEHLseEAKdfLRKCLRRDPKKRP-TADE 253
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
17-209 1.19e-41

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: 149.69  E-value: 1.19e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  17 VGRGGMAEVFRARDLRLDRLVAVKTLRSDLarDPTFQARFRREAQSAASLNHPSIIAVYDTGEDVidgvPIPYIVMEYVD 96
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIKKED--SSSLLEELLREIEILKKLNHPNIVKLYGVFEDE----NHLYLVMEYCE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  97 GRTLKELLEDNRRLLPERT-----LEITDGILRALAAaharGIVHRDIKPANVMLT-RQAEVKVMDFGIARAMNDAQATM 170
Cdd:cd00180  75 GGSLKDLLKENEGKLSEDEilrilLQILEGLEYLHSN----GIIHRDLKPENILLDsDNGKVKLADFGLSKLLTSDKSLL 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 72163465 171 TqtsQVIGTAQYLSPEQARGER-VDVRSDIYSTGCVLYEL 209
Cdd:cd00180 151 K---TIVGTPAYMAPEVLLGKGyYSEKSDIWSLGVILYEL 187
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
11-268 1.59e-41

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: 150.82  E-value: 1.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  11 YQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRSDLARDptfQARFRREAQSAASLNHPSII----AVYDTGEdvidgvp 86
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEK---KEKIINEIQILKKCKHPNIVkyygSYLKKDE------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  87 iPYIVMEYVDGRTLKELLEDNRRLLPERTLE-ITDGILRALAAAHARGIVHRDIKPANVMLTRQAEVKVMDFGIARAMND 165
Cdd:cd05122  72 -LWIVMEFCSGGSLKDLLKSTNQTLTESQIAyVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 166 AQATMTqtsqVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYqHVREEPiPPTELDPEipE 245
Cdd:cd05122 151 TKARNT----MVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKALF-KIATNG-PPGLRNPE--K 222
                       250       260
                ....*....|....*....|....*.
gi 72163465 246 WIE---AIVLRAMAKDREQRyQTAEE 268
Cdd:cd05122 223 WSDefkDFLKKCLQKNPEKR-PTAEQ 247
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
10-269 8.77e-36

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: 134.30  E-value: 8.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  10 RYQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRsdLARDPT-FQARFRREAQSAASLNHPSI---IAVYDTGEDVidgv 85
Cdd:cd06627   1 NYQLGDLIGRGAFGVVYKGLNLETGDFVAIKQIS--LEKIKEeALKSIMQEIDLLKNLKHPNIvkyIGSIETSDSL---- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  86 pipYIVMEYVDGRTLKELLEDNRRLlPERTL-----EITDGILRALAAaharGIVHRDIKPANVMLTRQAEVKVMDFGIA 160
Cdd:cd06627  75 ---YIILEYAENGSLRQIIKKFGPF-PESLVavyvyQVLQGLAYLHEQ----GVIHRDIKAANILTTKDGVVKLADFGVA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465 161 RAMNDAQatmTQTSQVIGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGDSPVSIAYQHVR-EEPIPPTEL 239
Cdd:cd06627 147 TKLNDVS---KDDASVVGTPYWMAPEVIEMSGASTASDIWSLGCTVIELLTGNPPYYDLNPMAALFRIVQdDHPPLPEGI 223
                       250       260       270
                ....*....|....*....|....*....|
gi 72163465 240 DPEIPEWIeaivLRAMAKDREQRyQTAEEM 269
Cdd:cd06627 224 SPELKDFL----MQCFQKDPNLR-PTAKQL 248
STKc_Nek6_Nek7 cd08224
Catalytic domain of the Protein Serine/Threonine Kinases, Never In Mitosis gene A-related ...
9-219 7.31e-35

Catalytic domain of the Protein Serine/Threonine Kinases, Never In Mitosis gene A-related kinase 6 and 7; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 6 (Nek6) and Nek7 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek6/7 subfamily 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173764 [Multi-domain]  Cd Length: 267  Bit Score: 132.17  E-value: 7.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465   9 GRYQLEAPVGRGGMAEVFRARDLRLDRLVAVKTLRSDLARDPTFQARFRREAQSAASLNHPSIIAVYDTgedVIDGVPIp 88
Cdd:cd08224   2 GNFKIEKKIGKGQFSVVYKAICLLDGRVVALKKVQIFEMMDAKARQDCLKEIDLLKQLDHPNVIKYLAS---FIENNEL- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72163465  89 YIVMEYVDGRTLKELLE---DNRRLLPERTL-----EITDGILRALAAAhargIVHRDIKPANVMLTRQAEVKVMDFGIA 160
Cdd:cd08224  78 NIVLELADAGDLSRMIKhfkKQKRLIPERTIwkyfvQLCSALEHMHSKR----IMHRDIKPANVFITATGVVKLGDLGLG 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 72163465 161 RAMndAQATMTQTSQViGTAQYLSPEQARGERVDVRSDIYSTGCVLYELLTGRPPFVGD 219
Cdd:cd08224 154 RFF--SSKTTAAHSLV-GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
18-269 4.87e-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 pl