NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|116624752|ref|YP_826908|]
View 

serine/threonine protein kinase [Candidatus Solibacter usitatus Ellin6076]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
8-268 5.64e-50

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: 177.69  E-value: 5.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDERLKRSVAIKVLR-HHENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMEL 86
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDlSNMSEKEREDALNEVKILKKLNHPNIIKYYESFEEKGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  87 ASGRTLAALVRDH-----PLRVEE----------ALDYASQLAsalaaahaggIVHRDIKPANIVVSESGTIKVLDFGIA 151
Cdd:cd08215   81 ADGGDLSQKIKKQkkegkPFPEEQildwfvqlclALKYLHSRK----------ILHRDIKPQNIFLTSNGLVKLGDFGIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 152 K-LEphgpsgdSTETAAPetaagSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLRD 230
Cdd:cd08215  151 KvLS-------STVDLAK-----TVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKG 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 116624752 231 QPRAIcelRAEVPPAVARIVNRCLEKDIALRyPSGTEL 268
Cdd:cd08215  219 QYPPI---PSQYSSELRNLVSSLLQKDPEER-PSIAQI 252
FGE-sulfatase super family cl19582
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
438-651 6.25e-19

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


The actual alignment was detected with superfamily member pfam03781:

Pssm-ID: 267935  Cd Length: 259  Bit Score: 87.17  E-value: 6.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  438 VAAGMVKVASQASWAAPNNLMP----LPDYFLDKFEVTNREYQQFVDSGGYRDakhwrhsflKDHREVPREQALLLFRDT 513
Cdd:pfam03781   8 IPGGSFEMGSAERTGNDNEAPAhdvtVRPFAIDKYPVTNAQYAAFVEATGYTT---------EVYPQWWAEVEGANWRHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  514 TGRPGPARwelgafpkGQADFPVSGVSWFEAAAYCESVGKT------LPTVHHWRKAA-------------AFDVFSEIL 574
Cdd:pfam03781  79 SGGLSDID--------DGADHPVTGVSWYDAVAYARWLGKRtgngyrLPTEAEWEYAArggskgrrypwgdELYPAGNIW 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  575 LFSNFSGTGPARVGANpGITT---------FGAYDMAGNVKEWCW------------------NQTGELRSILGGGW--N 625
Cdd:pfam03781 151 QGADFPNEHAGADSFN-GRTSpvgsfppnaLGLYDMAGNVWEWTSdwykphysfapydelsrdNFGGGYRVVRGGSWacS 229
                         250       260
                  ....*....|....*....|....*....
gi 116624752  626 EPSYAYRD---DDAQDPMKREVTYGVRCA 651
Cdd:pfam03781 230 VYPSRLRPafrGNCQTPGTRADDVGFRLV 258
PEGA super family cl17959
PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer ...
363-415 1.78e-03

PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer (surface layer) proteins. It is named after the characteristic PEGA sequence motif found in this domain. The secondary structure of this domain is predicted to be beta-strands [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16].


The actual alignment was detected with superfamily member pfam08308:

Pssm-ID: 116891  Cd Length: 71  Bit Score: 37.61  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 116624752  363 LTMTTTPPGVTVSyrpygdaaLPWQPVGRTPLENVRVPLAYMRVRLAKEGWEP 415
Cdd:pfam08308   4 LSVSSNPSGATVY--------IDGVYVGSTPVTLSDLPAGTHTLRLEKEGYED 48
FSH1 super family cl18428
Serine hydrolase (FSH1); This is a family of serine hydrolases.
813-925 4.38e-03

Serine hydrolase (FSH1); This is a family of serine hydrolases.


The actual alignment was detected with superfamily member pfam03959:

Pssm-ID: 252277  Cd Length: 209  Bit Score: 38.42  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  813 SVDYLEtrtDTQKDRLAYYGL---SVGGTFGALFLAL---------EPRLKTGILAAGglFGERPPPEADVlnFAPRVHV 880
Cdd:pfam03959  87 SLDYVR---DYIKENGPFDGIlgfSQGAALAAILASLleeglplesHPPLKFAILISG--FRPREPKYAEY--YSPPIQT 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 116624752  881 PVLMLNGRYDFVAPPatlQRPMFrwLGTA-EPDKRLIQFESGHMPP 925
Cdd:pfam03959 160 PSLHVIGELDTVVPE---ERSEK--LAEAcKNSATVLEHPGGHFVP 200
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-262 3.35e-60

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 205.84  E-value: 3.35e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752     9 YRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMELAS 88
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752    89 GRTLAALVRDHPLRVE-----------EALDYASQLasalaaahagGIVHRDIKPANIVVSESGTIKVLDFGIAKLEphg 157
Cdd:smart00220  81 GGDLFDLLKKRGRLSEdearfylrqilSALEYLHSK----------GIVHRDLKPENILLDEDGHVKLADFGLARQL--- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   158 psgdstetaAPETAAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLRDQPRAICE 237
Cdd:smart00220 148 ---------DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPP 218
                          250       260
                   ....*....|....*....|....*
gi 116624752   238 LRAEVPPAVARIVNRCLEKDIALRY 262
Cdd:smart00220 219 PEWDISPEAKDLIRKLLVKDPEKRL 243
COG3458 COG3458
Acetyl esterase (deacetylase) [Secondary metabolites biosynthesis, transport, and catabolism]
667-943 7.25e-09

Acetyl esterase (deacetylase) [Secondary metabolites biosynthesis, transport, and catabolism]


:

Pssm-ID: 225989 [Multi-domain]  Cd Length: 321  Bit Score: 57.06  E-value: 7.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 667 PPVRDYSTEKPVSDETFEIFRRMYAYDR-TPLNGKTESVDDSNEDWRKEKVSYSAaYGGERITAYLYLPRNAKPPYQTVL 745
Cdd:COG3458    9 EELKAYRPEREAPDDFDEFWKKTLEEARkVPPEPVLERSDFTLPRVEVYDVTFTG-YGGARIKGWLVLPRHEKGKLPAVV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 746 wVPGGYawmlrNSETGVGTEFFNFLLrTGRAVLYPVYQGTFERHVDNGGGPNARRD--WTIQFAKDVSRSVDYLETRTDT 823
Cdd:COG3458   88 -QFHGY-----GGRGGEWHDMLHWAV-AGYAVFVMDVRGQGSSSQDTADPPGGPSDpgFMTRGILDRKDTYYYRGVFLDA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 824 -------------QKDRLAYYGLSVGGTFGALFLALEPRLKTGI--------------LAAGGLFGE--------RPPPE 868
Cdd:COG3458  161 vraveilasldevDEERIGVTGGSQGGGLALAAAALDPRIKAVVadypflsdfpraieLATEGPYDEiqtyfkrhDPKEA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 869 A--------DVLNFAPRVHVPVLMLNGRYDFVAPPATlQRPMFRWLGTAEPDKRLIQFESGHMPPVEDlmREVLDWLDRY 940
Cdd:COG3458  241 EvfetlsyfDIVNLAARIKVPVLMSVGLMDPVCPPST-QFAAYNALTTSKTIEIYPYFAHEGGPGFQS--RQQVHFLKIL 317

                 ...
gi 116624752 941 LGP 943
Cdd:COG3458  318 FGL 320
 
Name Accession Description Interval E-value
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
8-268 5.64e-50

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: 177.69  E-value: 5.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDERLKRSVAIKVLR-HHENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMEL 86
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDlSNMSEKEREDALNEVKILKKLNHPNIIKYYESFEEKGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  87 ASGRTLAALVRDH-----PLRVEE----------ALDYASQLAsalaaahaggIVHRDIKPANIVVSESGTIKVLDFGIA 151
Cdd:cd08215   81 ADGGDLSQKIKKQkkegkPFPEEQildwfvqlclALKYLHSRK----------ILHRDIKPQNIFLTSNGLVKLGDFGIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 152 K-LEphgpsgdSTETAAPetaagSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLRD 230
Cdd:cd08215  151 KvLS-------STVDLAK-----TVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKG 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 116624752 231 QPRAIcelRAEVPPAVARIVNRCLEKDIALRyPSGTEL 268
Cdd:cd08215  219 QYPPI---PSQYSSELRNLVSSLLQKDPEER-PSIAQI 252
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
438-651 6.25e-19

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


Pssm-ID: 252159  Cd Length: 259  Bit Score: 87.17  E-value: 6.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  438 VAAGMVKVASQASWAAPNNLMP----LPDYFLDKFEVTNREYQQFVDSGGYRDakhwrhsflKDHREVPREQALLLFRDT 513
Cdd:pfam03781   8 IPGGSFEMGSAERTGNDNEAPAhdvtVRPFAIDKYPVTNAQYAAFVEATGYTT---------EVYPQWWAEVEGANWRHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  514 TGRPGPARwelgafpkGQADFPVSGVSWFEAAAYCESVGKT------LPTVHHWRKAA-------------AFDVFSEIL 574
Cdd:pfam03781  79 SGGLSDID--------DGADHPVTGVSWYDAVAYARWLGKRtgngyrLPTEAEWEYAArggskgrrypwgdELYPAGNIW 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  575 LFSNFSGTGPARVGANpGITT---------FGAYDMAGNVKEWCW------------------NQTGELRSILGGGW--N 625
Cdd:pfam03781 151 QGADFPNEHAGADSFN-GRTSpvgsfppnaLGLYDMAGNVWEWTSdwykphysfapydelsrdNFGGGYRVVRGGSWacS 229
                         250       260
                  ....*....|....*....|....*....
gi 116624752  626 EPSYAYRD---DDAQDPMKREVTYGVRCA 651
Cdd:pfam03781 230 VYPSRLRPafrGNCQTPGTRADDVGFRLV 258
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
12-157 1.38e-04

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 42.65  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  12 LEKLGQGGMGEVYRAE--------DERLKRSVAIKVLRHHENRDaalRFLQEARAASAL-----NHPnivQIYDLESHDG 78
Cdd:COG3642    1 MDLIKQGAEAIIYLTDflglpavvKERIPKRYRHPELDEKLRRE---RTRREARILAKAreagvPVP---IVYDVDPDNG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  79 rdFIVMELASGRTLAALVRDHPLRVEEALDYASQLASAlaaahaGGIVHRDIKPANIVVSESGTIkVLDFGIAK----LE 154
Cdd:COG3642   75 --LIVMEYIEGELLKDALEEARPDLLREVGRLVGKLHK------AGIVHGDLTTSNIILSGGRIY-FIDFGLGEfsdeVE 145

                 ...
gi 116624752 155 PHG 157
Cdd:COG3642  146 DKA 148
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
12-157 2.06e-04

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 42.20  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  12 LEKLGQGGMGEVYRAE--------DERLKRSVAIKVLRHHENRD---AALRFLQEARAAsALNHPnIVQIYDLEshdgRD 80
Cdd:PRK14879   1 MKLIKRGAEAEIYLGDflgikaviKWRIPKRYRHPELDERIRRErtrREARIMSRARKA-GVNVP-AVYFVDPE----NF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  81 FIVMELASGRTLAALVRDHPlrvEEALDYASQLASALAAAHAGGIVHRDIKPANIVVSEsGTIKVLDFGIAK----LEPH 156
Cdd:PRK14879  75 IIVMEYIEGEPLKDLINSNG---MEELELSREIGRLVGKLHSAGIIHGDLTTSNMILSG-GKIYLIDFGLAEfskdLEDR 150

                 .
gi 116624752 157 G 157
Cdd:PRK14879 151 A 151
PEGA pfam08308
PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer ...
363-415 1.78e-03

PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer (surface layer) proteins. It is named after the characteristic PEGA sequence motif found in this domain. The secondary structure of this domain is predicted to be beta-strands [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16].


Pssm-ID: 116891  Cd Length: 71  Bit Score: 37.61  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 116624752  363 LTMTTTPPGVTVSyrpygdaaLPWQPVGRTPLENVRVPLAYMRVRLAKEGWEP 415
Cdd:pfam08308   4 LSVSSNPSGATVY--------IDGVYVGSTPVTLSDLPAGTHTLRLEKEGYED 48
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
15-157 2.48e-03

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: 39.12  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   15 LGQGGMGEVYRAE--------DERLKRSVAIKVLRHHENRDaalRFLQEARAASAL-----NHPnivQIYDLESHDGRdf 81
Cdd:TIGR03724   2 IAKGAEAIIYLGDflglkaviKERVPKSYRHPELDERIRRE---RTRNEARLLSRArkagvNTP---VVYDVDPDNKT-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   82 IVMELASGRTLAALVRDHPLRVEEALDYASQLASAlaaahaGGIVHRDIKPANIVVSESGTIkVLDFGIAK----LEPHG 157
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIEEGNDELLREIGRLVGKLHK------AGIVHGDLTTSNIIVRDDKLY-LIDFGLGKysdeIEDKA 146
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
813-925 4.38e-03

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 252277  Cd Length: 209  Bit Score: 38.42  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  813 SVDYLEtrtDTQKDRLAYYGL---SVGGTFGALFLAL---------EPRLKTGILAAGglFGERPPPEADVlnFAPRVHV 880
Cdd:pfam03959  87 SLDYVR---DYIKENGPFDGIlgfSQGAALAAILASLleeglplesHPPLKFAILISG--FRPREPKYAEY--YSPPIQT 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 116624752  881 PVLMLNGRYDFVAPPatlQRPMFrwLGTA-EPDKRLIQFESGHMPP 925
Cdd:pfam03959 160 PSLHVIGELDTVVPE---ERSEK--LAEAcKNSATVLEHPGGHFVP 200
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
9-262 3.35e-60

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 205.84  E-value: 3.35e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752     9 YRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMELAS 88
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752    89 GRTLAALVRDHPLRVE-----------EALDYASQLasalaaahagGIVHRDIKPANIVVSESGTIKVLDFGIAKLEphg 157
Cdd:smart00220  81 GGDLFDLLKKRGRLSEdearfylrqilSALEYLHSK----------GIVHRDLKPENILLDEDGHVKLADFGLARQL--- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   158 psgdstetaAPETAAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLRDQPRAICE 237
Cdd:smart00220 148 ---------DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPP 218
                          250       260
                   ....*....|....*....|....*
gi 116624752   238 LRAEVPPAVARIVNRCLEKDIALRY 262
Cdd:smart00220 219 PEWDISPEAKDLIRKLLVKDPEKRL 243
COG3458 COG3458
Acetyl esterase (deacetylase) [Secondary metabolites biosynthesis, transport, and catabolism]
667-943 7.25e-09

Acetyl esterase (deacetylase) [Secondary metabolites biosynthesis, transport, and catabolism]


Pssm-ID: 225989 [Multi-domain]  Cd Length: 321  Bit Score: 57.06  E-value: 7.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 667 PPVRDYSTEKPVSDETFEIFRRMYAYDR-TPLNGKTESVDDSNEDWRKEKVSYSAaYGGERITAYLYLPRNAKPPYQTVL 745
Cdd:COG3458    9 EELKAYRPEREAPDDFDEFWKKTLEEARkVPPEPVLERSDFTLPRVEVYDVTFTG-YGGARIKGWLVLPRHEKGKLPAVV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 746 wVPGGYawmlrNSETGVGTEFFNFLLrTGRAVLYPVYQGTFERHVDNGGGPNARRD--WTIQFAKDVSRSVDYLETRTDT 823
Cdd:COG3458   88 -QFHGY-----GGRGGEWHDMLHWAV-AGYAVFVMDVRGQGSSSQDTADPPGGPSDpgFMTRGILDRKDTYYYRGVFLDA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 824 -------------QKDRLAYYGLSVGGTFGALFLALEPRLKTGI--------------LAAGGLFGE--------RPPPE 868
Cdd:COG3458  161 vraveilasldevDEERIGVTGGSQGGGLALAAAALDPRIKAVVadypflsdfpraieLATEGPYDEiqtyfkrhDPKEA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 869 A--------DVLNFAPRVHVPVLMLNGRYDFVAPPATlQRPMFRWLGTAEPDKRLIQFESGHMPPVEDlmREVLDWLDRY 940
Cdd:COG3458  241 EvfetlsyfDIVNLAARIKVPVLMSVGLMDPVCPPST-QFAAYNALTTSKTIEIYPYFAHEGGPGFQS--RQQVHFLKIL 317

                 ...
gi 116624752 941 LGP 943
Cdd:COG3458  318 FGL 320
Pkinase pfam00069
Protein kinase domain;
9-268 5.22e-46

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 166.65  E-value: 5.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752    9 YRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAALR-FLQEARAASALNHPNIVQIYDLESHDGRDFIVMELA 87
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKRSEKSKKDQtARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   88 SGRTLAALVRDHP-----------LRVEEALDYASQLasalaaahagGIVHRDIKPANIVVSESGTIKVLDFGIAKLePH 156
Cdd:pfam00069  81 EGGDLFDYLSRGGplsedeakkiaLQILRGLEYLHSN----------GIIHRDLKPENILLDENGVVKIADFGLAKK-LT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  157 GPSGDSTetaapetaagSFLGTVAYASPEQ-AQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPG---ILSKVLRDQP 232
Cdd:pfam00069 150 KSSSSLT----------TFVGTPEYMAPEVlLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDqlqLIRRILGPPL 219
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 116624752  233 RAICELRAEVPPAVARIVNRCLEKDIALRyPSGTEL 268
Cdd:pfam00069 220 EFDEPKSDSGSEEAKDLIKKCLNKDPSKR-PTAEEI 254
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
8-272 6.64e-46

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: 169.92  E-value: 6.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDerlKRSVAIKVLR--HHENRDAALRFLQEARAASALNHP-NIVQIYDLESHDGRDFIVM 84
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARD---RKLVALKVLAkkLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  85 ELASGRTLAALVRDH----PLRVEEALDYASQLASALAAAHAGGIVHRDIKPANIVVSESGT-IKVLDFGIAKLephgpS 159
Cdd:COG0515   78 EYVDGGSLEDLLKKIgrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKL-----L 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 160 GDSTETAAPETAAGSFLGTVAYASPEQAQG---RPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLR------- 229
Cdd:COG0515  153 PDPGSTSSIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelpt 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 116624752 230 --DQPRAICELRAEVPPAVARIVNRCLEKDIALRYPSGTELAADL 272
Cdd:COG0515  233 psLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDL 277
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
35-288 1.46e-32

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: 135.36  E-value: 1.46e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752    35 VAIKVLRHHENRDAAL--RFLQEARAASALNHPNIVQIYDL-ESHDGRDFIVMELASGRTLAA-LVRDHPLRVEEALDYA 110
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQraRFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREvLAADGALPAGETGRLM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   111 SQLASALAAAHAGGIVHRDIKPANIVVSESGT---IKVLDFGIAKLEPHgpSGDSTETAApeTAAGSFLGTVAYASPEQA 187
Cdd:TIGR03903   86 LQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTLLPG--VRDADVATL--TRTTEVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   188 QGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLRDQPRAIcelraevPPAVA-----RIVNRCLEKDIALRY 262
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSL-------PPWIAghplgQVLRKALNKDPRQRA 234
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 116624752   263 PSGTELA--------ADLTGC-RAAPAAGISNLSR 288
Cdd:TIGR03903  235 ASAPALAerfralelCALVGIlRMGEGAGREAIAA 269
pknD PRK13184
serine/threonine-protein kinase; Reviewed
6-272 1.97e-32

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 134.51  E-value: 1.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   6 IGNYRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHH--ENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIV 83
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlsENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  84 MELASGRTLAALVRD--------HPLRVEEA----LDYASQLASALAAAHAGGIVHRDIKPANIVVSESGTIKVLDFGIA 151
Cdd:PRK13184  81 MPYIEGYTLKSLLKSvwqkeslsKELAEKTSvgafLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 152 KLEpHGPSGDSTETAAPE--------TAAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGT---RAFDGDST 220
Cdd:PRK13184 161 IFK-KLEEEDLLDIDVDErnicyssmTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSfpyRRKKGRKI 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 116624752 221 PgilskvLRDQ---PRAICELRaEVPPAVARIVNRCLEKDIALRYPSGTELAADL 272
Cdd:PRK13184 240 S------YRDVilsPIEVAPYR-EIPPFLSQIAMKALAVDPAERYSSVQELKQDL 287
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
125-268 8.33e-18

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 86.46  E-value: 8.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 125 IVHRDIKPANIVVSESGTIKVLDFGIAKLEPHGPSGDSTETaapetaagsFLGTVAYASPEQAQGRPVDARSDIFSAGAV 204
Cdd:PTZ00283 164 MIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRT---------FCGTPYYVAPEIWRRKPYSKKADMFSLGVL 234
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116624752 205 MYEMLTGTRAFDGDSTPGILSKVL--RDQPraiceLRAEVPPAVARIVNRCLEKDIALRYPSGTEL 268
Cdd:PTZ00283 235 LYELLTLKRPFDGENMEEVMHKTLagRYDP-----LPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
460-608 2.40e-16

ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases) [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].


Pssm-ID: 234211 [Multi-domain]  Cd Length: 406  Bit Score: 81.22  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  460 LPDYFLDKFEVTNREYQQFVDSGGYRDAKHWrhsfLKDHREVPREQalllfrdttGRPGPARWE----------LGAFPK 529
Cdd:TIGR03440 200 VPPFEIDARPVTNGEYLEFIEDGGYRRPELW----LSDGWAWVQAE---------GWQAPLYWRrddgtwwvftLGGLRP 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  530 GQADFPVSGVSWFEAAAYCESVGKTLPTVHHWRKAAAFDVfseilLFSNFSGTGP-ARVGANPGITTfGAYDMAGNVKEW 608
Cdd:TIGR03440 267 LDPDAPVCHVSYYEADAYARWAGARLPTEAEWEKAARWGD-----APPNFAEANLgAPVGAYPAGAQ-GLGQLFGDVWEW 340
COG1262 COG1262
Uncharacterized conserved protein [Function unknown]
460-651 4.38e-16

Uncharacterized conserved protein [Function unknown]


Pssm-ID: 224182 [Multi-domain]  Cd Length: 314  Bit Score: 79.15  E-value: 4.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 460 LPDYFLDKFEVTNREYQQFVDSGGYRDAkhwrhsflkdhrevpreqalllFRDTTGRPGPARWElGAFPKGQADFPVSGV 539
Cdd:COG1262   85 VPPFEIDKYPVTNAQFARFVEAGGYTTA----------------------WEEDGEPVYPSYWK-GEGGRLRLEHPVVGV 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 540 SWFEAAAYCESVG-----KTLPTVHHWRKAA---------------------AFDVFSEILLFSNFSGTG-PARVGANPG 592
Cdd:COG1262  142 SWYDAQAYAAWLGvktgeYRLPTEAEWEYAAragtttdsypwgdelepglnaYAGTWEYLRAAAGWAREReTAPVGAFPP 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 593 ITTFGAYDMAGNVKEWCW----------------------------NQTGELRSILGGGWNEPSYAYRDD--DAQDPMKR 642
Cdd:COG1262  222 NAAYGLYDMHGNVWEWTAdwekewhydnygpapsdgsawydgnsgsKFFGSLRVVRGGSWASYPGVLRPAfrNFLVPDYR 301

                 ....*....
gi 116624752 643 EVTYGVRCA 651
Cdd:COG1262  302 QAHVGFRCA 310
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
14-268 3.31e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 71.01  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  14 KLGQGGMGEVYRAEDERLKRSVAIKVLrhHENRDAALRfLQEARAASAL---NHPNIVQIYDLESHDGRDFIVMELASGR 90
Cdd:PLN00034  81 RIGSGAGGTVYKVIHRPTGRLYALKVI--YGNHEDTVR-RQICREIEILrdvNHPNVVKCHDMFDHNGEIQVLLEFMDGG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  91 TL-------AALVRDHPLRVEEALDYASQLAsalaaahaggIVHRDIKPANIVVSESGTIKVLDFGIAKLephgpsgdST 163
Cdd:PLN00034 158 SLegthiadEQFLADVARQILSGIAYLHRRH----------IVHRDIKPSNLLINSAKNVKIADFGVSRI--------LA 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 164 ETAAPetaAGSFLGTVAYASPEQA-----QGRPVDARSDIFSAGAVMYEMLTGTRAF----DGDSTPGILSKVLRDQPra 234
Cdd:PLN00034 220 QTMDP---CNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAICMSQPP-- 294
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 116624752 235 icelraEVPPAVAR----IVNRCLEKDIALRyPSGTEL 268
Cdd:PLN00034 295 ------EAPATASRefrhFISCCLQREPAKR-WSAMQL 325
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
9-243 7.26e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 63.71  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   9 YRILEKLGQGGMGEVY---RAEDERlKRSVAIKVLRHHENRDAALRFLQEaraasaLNHPNIVQIYDLESHDGRDFIVME 85
Cdd:PHA03207  94 YNILSSLTPGSEGEVFvctKHGDEQ-RKKVIVKAVTGGKTPGREIDILKT------ISHRAIINLIHAYRWKSTVCMVMP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  86 LASGRTLAALVRDHPLRVEEALDYASQLASALAAAHAGGIVHRDIKPANIVVSESGTIKVLDFGIA-KLEPHgpsgdste 164
Cdd:PHA03207 167 KYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAcKLDAH-------- 238
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116624752 165 TAAPETAAGSflGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKvLRDQPRAICELRAEVP 243
Cdd:PHA03207 239 PDTPQCYGWS--GTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGKQVKSSSSQ-LRSIIRCMQVHPLEFP 314
Abhydrolase_5 pfam12695
Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase ...
743-922 8.18e-06

Alpha/beta hydrolase family; This family contains a diverse range of alpha/beta hydrolase enzymes.


Pssm-ID: 257229 [Multi-domain]  Cd Length: 145  Bit Score: 45.40  E-value: 8.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  743 TVLWVPGGYAWMLRNSEtgvgteFFNFLLRTGRAVLYPVYQGTferhvdnggGPNARRDWTIQFAKDVSRsvdyletrTD 822
Cdd:pfam12695   1 LVVLLHGAGGDPEAYAP------LARALASRGYNVLAPDYPGH---------GASLGAPDAEAVLADAAL--------LL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  823 TQKDRLAYYGLSVGGTFGALFLALEPRLKTGILAAgglfgerPPPEADVLNfapRVHVPVLMLNGRYDFVAPPATLQRpM 902
Cdd:pfam12695  58 IDPERIVLVGHSLGGAVALLLAARDPRIKGVVLLA-------PYPDTDALA---KLKVPVLIIHGTRDGVVPPEEAEA-L 126
                         170       180
                  ....*....|....*....|.
gi 116624752  903 FRWLGtaePDKRLIQFE-SGH 922
Cdd:pfam12695 127 YAALP---GPAELVVIEgAGH 144
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
839-927 4.40e-03

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate [Energy metabolism, Other].


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 38.49  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  839 FGALFLALEPRLKTGILAAgglFGERPPP----------EADVLNFAPRVHVPVLMLNGRYDFVAPPATLQRpmfrwLGT 908
Cdd:TIGR02427 146 FTPGFREAHPARLDLYRNM---LVRQPPDgyagccaairDADFRDRLGAIAVPTLCIAGDQDGSTPPELVRE-----IAD 217
                          90       100
                  ....*....|....*....|
gi 116624752  909 AEPDKRLIQFES-GHMPPVE 927
Cdd:TIGR02427 218 LVPGARFAEIRGaGHIPCVE 237
 
Name Accession Description Interval E-value
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
8-268 5.64e-50

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: 177.69  E-value: 5.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDERLKRSVAIKVLR-HHENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMEL 86
Cdd:cd08215    1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDlSNMSEKEREDALNEVKILKKLNHPNIIKYYESFEEKGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  87 ASGRTLAALVRDH-----PLRVEE----------ALDYASQLAsalaaahaggIVHRDIKPANIVVSESGTIKVLDFGIA 151
Cdd:cd08215   81 ADGGDLSQKIKKQkkegkPFPEEQildwfvqlclALKYLHSRK----------ILHRDIKPQNIFLTSNGLVKLGDFGIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 152 K-LEphgpsgdSTETAAPetaagSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILSKVLRD 230
Cdd:cd08215  151 KvLS-------STVDLAK-----TVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKG 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 116624752 231 QPRAIcelRAEVPPAVARIVNRCLEKDIALRyPSGTEL 268
Cdd:cd08215  219 QYPPI---PSQYSSELRNLVSSLLQKDPEER-PSIAQI 252
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
15-208 4.93e-43

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: 156.63  E-value: 4.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  15 LGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAALRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMELASGRTLAA 94
Cdd:cd00180    1 LGEGGFGTVYLARDKKTGKKVAIKIIKKEDSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  95 LVRDHPLRVEE------------ALDYASQLasalaaahagGIVHRDIKPANIVVSE-SGTIKVLDFGIAKLEPHGPSGD 161
Cdd:cd00180   81 LLKENEGKLSEdeilrillqileGLEYLHSN----------GIIHRDLKPENILLDSdNGKVKLADFGLSKLLTSDKSLL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 116624752 162 STetaapetaagsFLGTVAYASPEQAQGRP-VDARSDIFSAGAVMYEM 208
Cdd:cd00180  151 KT-----------IVGTPAYMAPEVLLGKGyYSEKSDIWSLGVILYEL 187
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
8-268 1.63e-40

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 150.78  E-value: 1.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAALRFLQ-EARAASALNHPNIVQIYDLESHDGRDF--IVM 84
Cdd:cd06606    1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSVELSGDSEEELEALErEIRILSSLQHPNIVRYYGSERDEEKNTlnIFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  85 ELASGRTLAAL-----------VRDHPLRVEEALDYASQLasalaaahagGIVHRDIKPANIVVSESGTIKVLDFGIAKl 153
Cdd:cd06606   81 EYVSGGSLSSLlkkfgklpepvIRKYTRQILEGLAYLHSN----------GIVHRDIKGANILVDSDGVVKLADFGCAK- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 154 ephgpsgdSTETAAPETAAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAF--------------DGDS 219
Cdd:cd06606  150 --------RLGDIETGEGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWselgnpmaalykigSSGE 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 116624752 220 TPGI---LSKVLRDqpraicelraevppavarIVNRCLEKDIALRyPSGTEL 268
Cdd:cd06606  222 PPEIpehLSEEAKD------------------FLRKCLRRDPKKR-PTADEL 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
9-268 1.52e-39

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: 148.12  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   9 YRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAAlRFLQEARAASALNHPNIVQIYDLESHDGRDFIVMELAS 88
Cdd:cd05122    2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKKE-KIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  89 GRTLAALVRDHPLRVEE------------ALDYASQLasalaaahagGIVHRDIKPANIVVSESGTIKVLDFGIAKleph 156
Cdd:cd05122   81 GGSLKDLLKSTNQTLTEsqiayvckellkGLEYLHSN----------GIIHRDIKAANILLTSDGEVKLIDFGLSA---- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 157 gpsgdsteTAAPETAAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFdGDSTP-GILSKVLRDQPrai 235
Cdd:cd05122  147 --------QLSDTKARNTMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPY-SELPPmKALFKIATNGP--- 214
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 116624752 236 CELR--AEVPPAVARIVNRCLEKDIALRyPSGTEL 268
Cdd:cd05122  215 PGLRnpEKWSDEFKDFLKKCLQKNPEKR-PTAEQL 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
10-268 1.04e-34

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis. MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling, MKK2 is involved in cold and salt stress signaling, MKK4/MKK5 participates in innate immunity, and MKK7 regulates basal and systemic acquired resistance.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 134.26  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  10 RILEKLGQGGMGEVYRAEDERLKRSVAIKVLrhHENRDAALR--FLQEARAASALNHPNIVQIYDLESHDGRDFIVMELA 87
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKI--HVDGDEEFRkqLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  88 SGRTLAALVRDHPLRVEE-----------ALDYASQLASalaaahaggIVHRDIKPANIVVSESGTIKVLDFGIakleph 156
Cdd:cd06623   82 DGGSLADLLKKVGKIPEPvlayiarqilkGLDYLHTKRH---------IIHRDIKPSNLLINSKGEVKIADFGI------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 157 gpSGDSTETAAPetaAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGILskvlrDQPRAIC 236
Cdd:cd06623  147 --SKVLENTLDQ---CNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFF-----ELMQAIC 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 116624752 237 ElrAEVPPAVARI--------VNRCLEKDIALRyPSGTEL 268
Cdd:cd06623  217 D--GPPPSLPAEEfspefrdfISACLQKDPKKR-PSAAEL 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
8-268 7.48e-33

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: 128.52  E-value: 7.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAAL-RFLQEARAASALNHPNIVQIYDLESHDGRDFIVMEL 86
Cdd:cd06627    1 NYQLGDLIGRGAFGVVYKGLNLETGDFVAIKQISLEKIKEEALkSIMQEIDLLKNLKHPNIVKYIGSIETSDSLYIILEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  87 ASGRTLAALV-RDHPLRVEEALDYASQLASALAAAHAGGIVHRDIKPANIVVSESGTIKVLDFGIAklephgpsgdsTET 165
Cdd:cd06627   81 AENGSLRQIIkKFGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGVVKLADFGVA-----------TKL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 166 AAPETAAGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRA-FDGDSTPGILSKVLRDQPRaiceLRAEVPP 244
Cdd:cd06627  150 NDVSKDDASVVGTPYWMAPEVIEMSGASTASDIWSLGCTVIELLTGNPPyYDLNPMAALFRIVQDDHPP----LPEGISP 225
                        250       260
                 ....*....|....*....|....
gi 116624752 245 AVARIVNRCLEKDIALRyPSGTEL 268
Cdd:cd06627  226 ELKDFLMQCFQKDPNLR-PTAKQL 248
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
8-257 1.58e-32

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: 128.47  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752   8 NYRILEKLGQGGMGEVYRAEDERLKRSVAIKVL-RHHENRDAALRF-LQEARAASALN-HPNIVQIYDLESHDGRDFIVM 84
Cdd:cd05581    2 DFKFGKIIGEGSFSTVVLAKEKETNKEYAIKILdKRQLIKEKKVKYvKIEKEVLTRLNgHPGIIKLYYTFQDEENLYFVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  85 ELASGRTLAALVRDHPLRVEE-----------ALDYASQLasalaaahagGIVHRDIKPANIVVSESGTIKVLDFGIAKL 153
Cdd:cd05581   82 EYAPNGELLQYIRKYGSLDEKctrfyaaeillALEYLHSK----------GIIHRDLKPENILLDKDMHIKITDFGTAKV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752 154 EPHGPSGDSTETAAPETA---------AGSFLGTVAYASPEQAQGRPVDARSDIFSAGAVMYEMLTGTRAFDGDSTPGIL 224
Cdd:cd05581  152 LDPNSSPESNKGDATNIDsqieknrrrFASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTF 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 116624752 225 SKVLR---DQPRAIcelraevPPAVARIVNRCLEKD 257
Cdd:cd05581  232 QKILKleySFPPNF-------PPDAKDLIEKLLVLD 260
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
12-268 4.15e-32

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK4 activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 126.68  E-value: 4.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116624752  12 LEKLGQGGMGEVYRAEDERLKRSVAIKVLRHHENRDAALRFLQ-EARAASALNHPNIVQIYDLESHDGRDFIVMELASGR 90
Cdd:cd06626    5 GNKIGGGTFGKVYTAVNLDTGELMAVKEIRIQDNDPKTIKEIAdEMKVLELLKHPNLVKYYGVE