NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|81428307|ref|YP_395307|]
View 

serine/threonine protein kinase [Lactobacillus sakei subsp. sakei 23K]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

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 ...
361-422 6.90e-16

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: 72.95  E-value: 6.90e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81428307 361 TVPDLTDMTQQNAESALTDKKLKVGTVQKTTSQKYSKGHVIRTTPKAGLSVKSKSTVNLIVS 422
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
429-490 1.60e-11

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: 60.62  E-value: 1.60e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81428307 429 KIKDYTNQAYSDVRDALKDKGLKVKR-KYQSSSEVSPGLIIDQSIAAGKRVVPsKTTITLTVS 490
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVvTEEYSDDVPKGTVISQSPAAGTKVKK-GSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
500-557 4.31e-06

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: 44.83  E-value: 4.31e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307 500 NLSNYTKQGIQDYAAQNGLTVVFSEEYSS-SISEGMVISQSPASGTMVQEGDSVSVILS 557
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKVGVVTEEYSdDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
11-259 5.12e-67

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: 221.22  E-value: 5.12e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  11 RYKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDLRNDPSTVRRFtREALATTELNHPNIVSIYDVGEENSMQYIIME 90
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDLSNMSEKEREDAL-NEVKILKKLNHPNIIKYYESFEEKGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  91 YIKGTDL----KKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETaMT 166
Cdd:cd08215  80 YADGGDLsqkiKKQKKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLSST-VD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 167 QTNTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQDEVPPVRNydpRIPQALENVV 246
Cdd:cd08215 159 LAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPIPS---QYSSELRNLV 235
                       250
                ....*....|...
gi 81428307 247 LKATAKDPDERYS 259
Cdd:cd08215 236 SSLLQKDPEERPS 248
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-264 9.18e-83

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 262.85  E-value: 9.18e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307     12 YKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDlrNDPSTVRRFTREALATTELNHPNIVSIYDVGEENSMQYIIMEY 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307     92 IKGTDLKKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETAMtqTNTL 171
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    172 LGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQDEVPPVRNYDPRIPQALENVVLKATA 251
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|...
gi 81428307    252 KDPDERYSGVDAM 264
Cdd:smart00220 237 KDPEKRLTAEEAL 249
 
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 ...
361-422 6.90e-16

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: 72.95  E-value: 6.90e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81428307 361 TVPDLTDMTQQNAESALTDKKLKVGTVQKTTSQKYSKGHVIRTTPKAGLSVKSKSTVNLIVS 422
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
429-490 1.60e-11

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: 60.62  E-value: 1.60e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81428307 429 KIKDYTNQAYSDVRDALKDKGLKVKR-KYQSSSEVSPGLIIDQSIAAGKRVVPsKTTITLTVS 490
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVvTEEYSDDVPKGTVISQSPAAGTKVKK-GSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
500-557 4.31e-06

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: 44.83  E-value: 4.31e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307 500 NLSNYTKQGIQDYAAQNGLTVVFSEEYSS-SISEGMVISQSPASGTMVQEGDSVSVILS 557
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKVGVVTEEYSdDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
11-259 5.12e-67

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: 221.22  E-value: 5.12e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  11 RYKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDLRNDPSTVRRFtREALATTELNHPNIVSIYDVGEENSMQYIIME 90
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDLSNMSEKEREDAL-NEVKILKKLNHPNIIKYYESFEEKGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  91 YIKGTDL----KKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETaMT 166
Cdd:cd08215  80 YADGGDLsqkiKKQKKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLSST-VD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 167 QTNTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQDEVPPVRNydpRIPQALENVV 246
Cdd:cd08215 159 LAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPIPS---QYSSELRNLV 235
                       250
                ....*....|...
gi 81428307 247 LKATAKDPDERYS 259
Cdd:cd08215 236 SSLLQKDPEERPS 248
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
360-423 1.92e-11

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: 60.32  E-value: 1.92e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81428307   360 VTVPDLTDMTQQNAESALTDKKLKVGTVQKTTSqKYSKGHVIRTTPKAGLSVKSKSTVNLIVSS 423
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSD-DVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
428-491 4.69e-11

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: 59.17  E-value: 4.69e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81428307   428 YKIKDYTNQAYSDVRDALKDKGLKVKRKYQSSSEVSPGLIIDQSIAAGKRvVPSKTTITLTVSS 491
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTK-VKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
426-491 5.43e-11

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 59.24  E-value: 5.43e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81428307    426 QKYKIKDYTNQAYSDVRDALKDKGLKVKRKYQSSSEVSPGLIIDQSIAAGKRVVPSkTTITLTVSS 491
Cdd:smart00740   3 EKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPG-SKVTLTVSK 67
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
15-157 6.44e-11

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 61.14  E-value: 6.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  15 IRPIGEGGMANVYLAQdlILDRQVAVKVL--------RLD--LRNdpstvRRFTREA--LATTELNHPNIVSIYDVgEEN 82
Cdd:COG3642   1 MDLIKQGAEAIIYLTD--FLGLPAVVKERipkryrhpELDekLRR-----ERTRREAriLAKAREAGVPVPIVYDV-DPD 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81428307  83 SMQyIIMEYIKGTDLKKYIVEHFPipyqrviDIMTQILSAVQNAHAHNIIHRDLKPQNILVdEDGNIKISDFGIA 157
Cdd:COG3642  73 NGL-IVMEYIEGELLKDALEEARP-------DLLREVGRLVGKLHKAGIVHGDLTTSNIIL-SGGRIYFIDFGLG 138
PASTA smart00740
PASTA domain;
356-423 1.42e-10

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 58.09  E-value: 1.42e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81428307    356 QGSEVTVPDLTDMTQQNAESALTDKKLKVGTVQKTTSqKYSKGHVIRTTPKAGLSVKSKSTVNLIVSS 423
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALGLKVEVVEEYSS-DGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
11-213 1.94e-10

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 61.12  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   11 RYKIIRPIGEGGMANVYLAQ---DLILDRQVAVKVLRLDLRNDPSTV----RRFTREALAT----TELNHPNIVSIYDVG 79
Cdd:PHA02882  13 EWKIDKLIGCGGFGCVYETQcasDHCINNQAVAKIENLENETIVMETlvynNIYDIDKIALwkniHNIDHLGIPKYYGCG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   80 --EENSMQY--IIME--YIKGTDLKKYIVEHfpiPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISD 153
Cdd:PHA02882  93 sfKRCRMYYrfILLEklVENTKEIFKRIKCK---NKKLIKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIID 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81428307  154 FGIAIAL------SETAMTQTNTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEG 213
Cdd:PHA02882 170 YGIASHFiihgkhIEYSKEQKDLHRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKG 235
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
18-157 4.73e-09

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: 55.30  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    18 IGEGGMANVYLAQdlILDRQVAVKV--------LRLDLR-NDPSTVR--RFTREALATTeLNHPnivSIYDVGEENSMqy 86
Cdd:TIGR03724   2 IAKGAEAIIYLGD--FLGLKAVIKErvpksyrhPELDERiRRERTRNeaRLLSRARKAG-VNTP---VVYDVDPDNKT-- 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81428307    87 IIMEYIKGTDLKkYIVEHFPIPYQRVIDIMTQILsavqnaHAHNIIHRDLKPQNILVDEDGNIKIsDFGIA 157
Cdd:TIGR03724  74 IVMEYIEGKPLK-DVIEEGNDELLREIGRLVGKL------HKAGIVHGDLTTSNIIVRDDKLYLI-DFGLG 136
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
15-157 1.03e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 51.45  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   15 IRPIGEGGMANVYLAQdlILDRQVAVKVL--------RLD--LRndpstVRRFTREA--LATTELNHPNIVSIYDVGEEN 82
Cdd:PRK14879   1 MKLIKRGAEAEIYLGD--FLGIKAVIKWRipkryrhpELDerIR-----RERTRREAriMSRARKAGVNVPAVYFVDPEN 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81428307   83 SMqyIIMEYIKGTDLKKYIVEHFPIPYQ--RVIDIMTQILsavqnaHAHNIIHRDLKPQNILVdEDGNIKISDFGIA 157
Cdd:PRK14879  74 FI--IVMEYIEGEPLKDLINSNGMEELElsREIGRLVGKL------HSAGIIHGDLTTSNMIL-SGGKIYLIDFGLA 141
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
500-558 1.55e-06

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: 46.07  E-value: 1.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307   500 NLSNYTKQGIQDYAAQNGLTVVFSEEYSSSISEGMVISQSPASGTMVQEGDSVSVILSK 558
Cdd:pfam03793   5 DVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
500-558 2.09e-06

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 45.76  E-value: 2.09e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307    500 NLSNYTKQGIQDYAAQNGLTVVFSEEYSSSISEGMVISQSPASGTMVQEGDSVSVILSK 558
Cdd:smart00740   9 DVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
97-211 5.48e-04

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 258671  Cd Length: 289  Bit Score: 40.86  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    97 LKKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDF------GIAIALSETAMTQT-N 169
Cdd:pfam14531 133 LDSHSTFHKSLEHAARLLLTLQLIRLAAGLQHRGLVHGDFRPDNFFLDQKGGVFLGGFtalvraGTKVVVSEVDVAFApP 212
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 81428307   170 TLLGSVHYLSPEQARGSMATkrsDIYSLGIVLYELLTGMVPF 211
Cdd:pfam14531 213 ELFASRGYTGKNTTTMTHKT---DAWQLGLVIYRIWCLRLPF 251
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
133-257 2.40e-03

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: 38.15  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    133 HRDLKPQNILVDEDGNIKIsdFGiaialSETAMTQTNTLLGSVhYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFE 212
Cdd:smart00750  34 HRQAKSGNILLTWDGLLKL--DG-----SVAFKTPEQSRPDPY-FMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYN 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 81428307    213 GESAVS----IAIKHFQDEVPPVRNYD------PRIPQALENVVLKATAKDPDER 257
Cdd:smart00750 106 EERELSaileILLNGMPADDPRDRSNLegvsaaRSFEDFMRLCASRLPQRREAAN 160
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-264 9.18e-83

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 262.85  E-value: 9.18e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307     12 YKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDlrNDPSTVRRFTREALATTELNHPNIVSIYDVGEENSMQYIIMEY 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307     92 IKGTDLKKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETAMtqTNTL 171
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEK--LTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    172 LGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQDEVPPVRNYDPRIPQALENVVLKATA 251
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|...
gi 81428307    252 KDPDERYSGVDAM 264
Cdd:smart00220 237 KDPEKRLTAEEAL 249
Pkinase pfam00069
Protein kinase domain;
12-264 4.69e-71

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 232.14  E-value: 4.69e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    12 YKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDlRNDPSTVRRFTREALATTELNHPNIVSIYDVGEENSMQYIIMEY 91
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    92 IKGTDLKKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETAmTQTNTL 171
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKKLTKSS-SSLTTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   172 LGSVHYLSPEQ-ARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQD---EVPPVRNYDPRIPQALENVVL 247
Cdd:pfam00069 159 VGTPEYMAPEVlLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRIlgpPLEFDEPKSDSGSEEAKDLIK 238
                         250
                  ....*....|....*..
gi 81428307   248 KATAKDPDERYSGVDAM 264
Cdd:pfam00069 239 KCLNKDPSKRPTAEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
12-297 6.79e-64

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: 217.30  E-value: 6.79e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  12 YKIIRPIGEGGMANVYLAQDLildRQVAVKVLRLDLRNDPSTVRRFTREALATTELNHP-NIVSIYDVGEENSMQYIIME 90
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  91 YIKGTDLKKYIVEHF---PIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGN-IKISDFGIAIALSETAMT 166
Cdd:COG0515  79 YVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 167 Q-----TNTLLGSVHYLSPEQARGSM---ATKRSDIYSLGIVLYELLTGMVPFEGESAVSI---AIKHFQDEVPPVRNYD 235
Cdd:COG0515 159 SsipalPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKNSSAtsqTLKIILELPTPSLASP 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81428307 236 PR------IPQALENVVLKATAKDPDERYSGVDAMMADLATSLSASRAHEPKFVPSKADDLSETKVIP 297
Cdd:COG0515 239 LSpsnpelISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPP 306
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-275 2.70e-52

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 192.68  E-value: 2.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   10 GRYKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDLRNDPSTVRRFTREALATTELNHPNIVSIYDVGEENSMQYIIM 89
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   90 EYIKGTDLK-------------KYIVEHFPIPyqRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGI 156
Cdd:PRK13184  82 PYIEGYTLKsllksvwqkeslsKELAEKTSVG--AFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  157 AIALSE-----------------TAMTQTNTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSI 219
Cdd:PRK13184 160 AIFKKLeeedlldidvdernicySSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307  220 AIKH---FQDEVPPVRNydprIPQALENVVLKATAKDPDERYSGVDAMMADLATSLSAS 275
Cdd:PRK13184 240 SYRDvilSPIEVAPYRE----IPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGS 294
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
348-560 2.15e-39

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 146.40  E-value: 2.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 348 ATVIAFAVQGSEVTVPDLTDMTQQNAESALTDKKLKVGTVQKTtSQKYSKGHVIRTTPKAGLSVKSKSTVNLIVSSGRQK 427
Cdd:COG2815  14 LLATFFPVSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRERE-SDKVPEGKVIRTDPKAGTVVKQGSKVTLFVSTGAQY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 428 YKIKDYTNQAYSDVRDALKDKGLK--VKRKYQSSSEVSPGLIIDQSIAAGKRVVPSKTtITLTVSSGKPGFALHNLSNYT 505
Cdd:COG2815  93 ITVPDVVGLTIEEAVAKLKAYGLNlsKITQEEVSDEVPAGTVISQSPSAGTEVKPGET-VKLTVSKGPETITVPDLVGMT 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 81428307 506 KQGIQDYAAQNGLTVVFSEEYSSSISEGMVISQSPASGTMVQEGDSVSVILSKGE 560
Cdd:COG2815 172 YDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGA 226
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
37-257 5.06e-39

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: 153.08  E-value: 5.06e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307     37 QVAVKVLRLDLRNDPSTVRRFTREALATTELNHPNIVSIYDVGE-ENSMQYIIMEYIKGTDLKKYIVEHFPIPYQRVIDI 115
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307    116 MTQILSAVQNAHAHNIIHRDLKPQNILVDEDG---NIKISDFGIAIALS------ETAMTQTNTLLGSVHYLSPEQARGS 186
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGTLLPgvrdadVATLTRTTEVLGTPTYCAPEQLRGE 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81428307    187 MATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQdevpPVrnyDPRIPQALE-----NVVLKATAKDPDER 257
Cdd:TIGR03903  165 PVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLS----PV---DVSLPPWIAghplgQVLRKALNKDPRQR 233
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
18-264 1.36e-27

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 113.32  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   18 IGEGGMANVYLAQDLILDRQVAVKVLRL-DLRNDPSTVRR--------FT--REALATTELNHPNIVSIYDVGEENSMQY 86
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIiEISNDVTKDRQlvgmcgihFTtlRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   87 IIMEYIKGtDLKKyIVEH---FPIPYQRVIdiMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIA------ 157
Cdd:PTZ00024  97 LVMDIMAS-DLKK-VVDRkirLTESQVKCI--LLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLArrygyp 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  158 ---IALSETAMTQTNTLLGS----VHYLSPEQARGSMATKRS-DIYSLGIVLYELLTGMVPFEGESAVSIAIKHF----- 224
Cdd:PTZ00024 173 pysDTLSKDETMQRREEMTSkvvtLWYRAPELLMGAEKYHFAvDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFellgt 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307  225 --QDEVPPVRN------YDPRIPQALENVVLKATAK-----------DPDERYSGVDAM 264
Cdd:PTZ00024 253 pnEDNWPQAKKlplyteFTPRKPKDLKTIFPNASDDaidllqsllklNPLERISAKEAL 311
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
15-264 6.24e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 111.84  E-value: 6.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   15 IRPIGEGGMANVYLAQDLILDRQVAVKVLrldLRNDPSTVRR-FTREALATTELNHPNIVSIYDVGEENSMQYIIMEYIK 93
Cdd:PLN00034  79 VNRIGSGAGGTVYKVIHRPTGRLYALKVI---YGNHEDTVRRqICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   94 GTDLKKYIVEHfpipYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETaMTQTNTLLG 173
Cdd:PLN00034 156 GGSLEGTHIAD----EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQT-MDPCNSSVG 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  174 SVHYLSPEQA-----RGSMATKRSDIYSLGIVLYELLTGMVPF----EGE-SAVSIAIKHFQDEVPPvrnydPRIPQALE 243
Cdd:PLN00034 231 TIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQGDwASLMCAICMSQPPEAP-----ATASREFR 305
                        250       260
                 ....*....|....*....|.
gi 81428307  244 NVVLKATAKDPDERYSGVDAM 264
Cdd:PLN00034 306 HFISCCLQREPAKRWSAMQLL 326
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
68-212 1.33e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 91.46  E-value: 1.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307   68 NHPNIVSIYDVGEENSMQYIIMEYIKGTDLKKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDE-D 146
Cdd:PHA03390  67 DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaK 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81428307  147 GNIKISDFGiaiaLSETAMTQTnTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFE 212
Cdd:PHA03390 147 DRIYLCDYG----LCKIIGTPS-CYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK 207
 
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 ...
361-422 6.90e-16

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: 72.95  E-value: 6.90e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81428307 361 TVPDLTDMTQQNAESALTDKKLKVGTVQKTTSQKYSKGHVIRTTPKAGLSVKSKSTVNLIVS 422
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
429-490 1.60e-11

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: 60.62  E-value: 1.60e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81428307 429 KIKDYTNQAYSDVRDALKDKGLKVKR-KYQSSSEVSPGLIIDQSIAAGKRVVPsKTTITLTVS 490
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVvTEEYSDDVPKGTVISQSPAAGTKVKK-GSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
500-557 4.31e-06

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: 44.83  E-value: 4.31e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 81428307 500 NLSNYTKQGIQDYAAQNGLTVVFSEEYSS-SISEGMVISQSPASGTMVQEGDSVSVILS 557
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKVGVVTEEYSdDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
11-259 5.12e-67

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: 221.22  E-value: 5.12e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  11 RYKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDLRNDPSTVRRFtREALATTELNHPNIVSIYDVGEENSMQYIIME 90
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDLSNMSEKEREDAL-NEVKILKKLNHPNIIKYYESFEEKGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  91 YIKGTDL----KKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETaMT 166
Cdd:cd08215  80 YADGGDLsqkiKKQKKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFGISKVLSST-VD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 167 QTNTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQDEVPPVRNydpRIPQALENVV 246
Cdd:cd08215 159 LAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYPPIPS---QYSSELRNLV 235
                       250
                ....*....|...
gi 81428307 247 LKATAKDPDERYS 259
Cdd:cd08215 236 SSLLQKDPEERPS 248
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
18-204 3.38e-59

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: 199.00  E-value: 3.38e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  18 IGEGGMANVYLAQDLILDRQVAVKVLRLDlrNDPSTVRRFTREALATTELNHPNIVSIYDVGEENSMQYIIMEYIKGTDL 97
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  98 KKYIVEHF-PIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDED-GNIKISDFGIAIALSETaMTQTNTLLGSV 175
Cdd:cd00180  79 KDLLKENEgKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDnGKVKLADFGLSKLLTSD-KSLLKTIVGTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 81428307 176 HYLSPEQARGSM-ATKRSDIYSLGIVLYEL 204
Cdd:cd00180 158 AYMAPEVLLGKGyYSEKSDIWSLGVILYEL 187
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
11-257 4.60e-53

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: 183.53  E-value: 4.60e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  11 RYKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDlRNDPSTVRRFTREALATTELNHPNIVSIY--DVGEENSMQYII 88
Cdd:cd06606   1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSVELS-GDSEEELEALEREIRILSSLQHPNIVRYYgsERDEEKNTLNIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  89 MEYIKGTDLKKYIvEHF-PIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETAMT- 166
Cdd:cd06606  80 LEYVSGGSLSSLL-KKFgKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLGDIETGe 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 167 QTNTLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKH--FQDEVPPvrnYDPRIPQALEN 244
Cdd:cd06606 159 GTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSELGNPMAALYKigSSGEPPE---IPEHLSEEAKD 235
                       250
                ....*....|...
gi 81428307 245 VVLKATAKDPDER 257
Cdd:cd06606 236 FLRKCLRRDPKKR 248
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
12-257 1.71e-45

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: 161.99  E-value: 1.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  12 YKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDLRNDPSTVrrfTREALATTELNHPNIVSIYDVGEENSMQYIIMEY 91
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKKEKI---INEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  92 IKGTDLKKyIVEHF--PIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETamTQTN 169
Cdd:cd05122  79 CSGGSLKD-LLKSTnqTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDT--KARN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 170 TLLGSVHYLSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVS----IAIKHFqdevPPVRNyDPRIPQALENV 245
Cdd:cd05122 156 TMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKalfkIATNGP----PGLRN-PEKWSDEFKDF 230
                       250
                ....*....|..
gi 81428307 246 VLKATAKDPDER 257
Cdd:cd05122 231 LKKCLQKNPEKR 242
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine ...
12-268 4.88e-45

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Cyclin-Dependent protein Kinase (CDK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CDK-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. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH.


Pssm-ID: 173733 [Multi-domain]  Cd Length: 282  Bit Score: 161.88  E-value: 4.88e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  12 YKIIRPIGEGGMANVYLAQDLILDRQVAVKVLRLDLRND--PSTVrrfTREALATTELNHPNIVSIYDVGEENSMQYIIM 89
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKARDKKTGEIVALKKIRLDNEEEgiPSTA---LREISLLKELKHPNIVKLLDVIHTERKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  90 EYIKgTDLKKYIVEHF-PIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETAMTQT 168
Cdd:cd07829  78 EYCD-MDLKKYLDKRPgPLSPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNILINRDGVLKLADFGLARAFGIPLRTYT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 169 NT-----------LLGSVHYLSPeqargsmatkrSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQ------DEVPP- 230
Cdd:cd07829 157 HEvvtlwyrapeiLLGSKHYSTA-----------VDIWSVGCIFAEMITGKPLFPGDSEIDQLFKIFQilgtptEESWPg 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 81428307 231 ---VRNYDPRIPqalenvvlKATAKDPDERYSGVDAMMADL 268
Cdd:cd07829 226 vtkLPDYKPTFP--------KFPPKDLEKVLPRLDPEGIDL 258
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
18-257 5.66e-45

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: 160.38  E-value: 5.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  18 IGEGGMANVYLAQDLILDRQVAVKVLRLDLRNDPSTVRRFTREALATTELNHPNIVSIYDVGEENSMQYIIMEYIKGTDL 97
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLKKKKIIKRKEVEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVLEYAPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  98 KKYIVEHFPIPYQRVIDIMTQILSAVQNAHAHNIIHRDLKPQNILVDEDGNIKISDFGIAIALSETaMTQTNTLLGSVHY 177
Cdd:cd05123  81 FSHLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLTDFGLAKELSSE-GSRTNTFCGTPEY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307 178 LSPEQARGSMATKRSDIYSLGIVLYELLTGMVPFEGESAVSIAIKHFQDEVppvrNYDPRIPQALENVVLKATAKDPDER 257
Cdd:cd05123 160 LAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAEDRKEIYEKILKDPL----RFPEFLSPEARDLISGLLQKDPTKR 235
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
12-264 4.81e-44

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: 158.90  E-value: 4.81e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81428307  12 YKIIRPIGEGGMANVYLAQDLILDRQVAVKVL---RLDLRNDPSTVrrfTREALATTELN-HPNIVSIYDVGEENSMQYI 87
Cdd:cd05581   3 FKFGKIIGEGSFSTVVLAKEKETNKEY