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Conserved domains on  [gi|29831260|ref|NP_825894|]
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serine/threonine protein kinase [Streptomyces avermitilis MA-4680 = NBRC 14893]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
29-269 3.01e-41

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 150.08  E-value: 3.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLARS-ASGLRLAVKVVHAQyaQDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLFIPGPTL 107
Cdd:cd00180   1 LGEGGFGTVYLARDkKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 108 AEHVKRNGA-LPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP--KVIDFGISRPSDSElRTETGKLIGTP 184
Cdd:cd00180  79 KDLLKENEGkLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGkvKLADFGLSKLLTSD-KSLLKTIVGTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 185 PFMAPEQFRRPREVGPAADVFALGsvivhaatgsgpfdsdspyLVAYQVvhdepdltgvpEELAELVAGCLAKEPDDRPT 264
Cdd:cd00180 158 AYMAPEVLLGKGYYSEKSDIWSLG-------------------VILYEL-----------PELKDLIRKMLQKDPEKRPS 207

                ....*
gi 29831260 265 PDELM 269
Cdd:cd00180 208 AKEIL 212
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
416-725 1.65e-22

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


:

Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 98.56  E-value: 1.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 416 RPGVLAAAVDPADGKVLWSRGDAKRHSDGTVRPPVLSGGLLHVVSEGGKrLAALDPATGKTRWSHDL---AAYGGRFAQV 492
Cdd:cd10276   1 PPTDLPEPTPEFDPEVLWSKSVGNGGMAGIDLTPVVAGDMVYAADANGQ-VSAFNATTGKIIWETSLsgkGFLGGTPAVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 493 GGVVLLTGADARVTALDAATGEEKWRRRIPGQPQPAFVSYGDGLAYAVAAAGsgtKVAAVDPESGATRWQRRFD-GVLSL 571
Cdd:cd10276  80 NGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPTYADGKIYVGTGDG---RLYYCNAETGKVVWNRTSTaPELSL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 572 ------VGAHDGAVWFAST------TADsDTDAVVRYDVTRRTVRRVGLRFPLQGAQAVVRKDTVYVLANGGALVAVDTR 639
Cdd:cd10276 157 rggaapVGAYDVVFVGDGNgtvvalNTG-TGVDIWEFSVSEPRGRTELPRMIDSSVTYVVVGGYLYSTSYQGYLVALDFE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 640 TSKELWRLETSvSFASAPVAAGDRVYFAGADGRLLAVDASKG-------VLLGQTKA----------------------- 689
Cdd:cd10276 236 SGQFLWSRKAS-GGTSTSTDANGRVYVGDGEGSLYCLDASTGdelwsqtVLLGRVLSspaiyvgvyiyvtdnaegylycl 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 29831260 690 -RLGGA------HGSLVSGLPSPVAADGKVYSAAPDGSLFAVD 725
Cdd:cd10276 315 kDNDGLtvarveVDYSQYILQGPAVSDGWLYYGTDDGYLYALT 357
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-270 4.68e-50

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.80  E-value: 4.68e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260     23 YLLEAALGSGGMGVVHLARS-ASGLRLAVKVVHAQyaQDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLF 101
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    102 IPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFGISRPSDSELRTETgkL 180
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTT--F 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    181 IGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVV-----HDEPDLTGVPEELAELVAGCL 255
Cdd:smart00220 157 VGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIgkpkpPFPPPEWDISPEAKDLIRKLL 235
                          250
                   ....*....|....*
gi 29831260    256 AKEPDDRPTPDELMT 270
Cdd:smart00220 236 VKDPEKRLTAEEALQ 250
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
422-681 6.34e-29

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


:

Pssm-ID: 257688 [Multi-domain]  Cd Length: 237  Bit Score: 115.95  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   422 AAVDPADGKVLWSRGDAKRHSDGTVRPPVLSGGLLHVVSEGGkRLAALDPATGKTRWSHDL-AAYGGRFAQVGGVVLLTG 500
Cdd:pfam13360   6 SALDAATGKVLWRVDLGPAAGTALGGGVAVDGGRLYVATGKG-ELVALDAADGKLLWRKDLsGEILGAPLVAGGRVYVVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   501 ADARVTALDAATGEEKWRRRIPGQPQ-----PAFVSYGDglayAVAAAGSGTKVAAVDPESGATRWQRRfdgvlslvgah 575
Cdd:pfam13360  85 ADGSLYALDAKTGKLLWSYQRSLPPLtlrgsSSPAIVGD----TVIVGFSSGKLVALDPKTGKVLWEAP----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   576 dgavwFASTTADSDTDAVVryDVTrrtvrrvglrfplqgAQAVVRKDTVYVLANGGALVAVDTRTSKELWRLEtsVSFAS 655
Cdd:pfam13360 150 -----VARPRGGSEIERLV--DIT---------------GTPVVDGGRVYASSYQGRLVAIDLATGKRLWSRP--ISSVN 205
                         250       260
                  ....*....|....*....|....*.
gi 29831260   656 APVAAGDRVYFAGADGRLLAVDASKG 681
Cdd:pfam13360 206 GPAVDGGVLFVVDDDGELVALDRATG 231
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
29-269 3.01e-41

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 150.08  E-value: 3.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLARS-ASGLRLAVKVVHAQyaQDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLFIPGPTL 107
Cdd:cd00180   1 LGEGGFGTVYLARDkKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 108 AEHVKRNGA-LPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP--KVIDFGISRPSDSElRTETGKLIGTP 184
Cdd:cd00180  79 KDLLKENEGkLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGkvKLADFGLSKLLTSD-KSLLKTIVGTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 185 PFMAPEQFRRPREVGPAADVFALGsvivhaatgsgpfdsdspyLVAYQVvhdepdltgvpEELAELVAGCLAKEPDDRPT 264
Cdd:cd00180 158 AYMAPEVLLGKGYYSEKSDIWSLG-------------------VILYEL-----------PELKDLIRKMLQKDPEKRPS 207

                ....*
gi 29831260 265 PDELM 269
Cdd:cd00180 208 AKEIL 212
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
416-725 1.65e-22

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 98.56  E-value: 1.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 416 RPGVLAAAVDPADGKVLWSRGDAKRHSDGTVRPPVLSGGLLHVVSEGGKrLAALDPATGKTRWSHDL---AAYGGRFAQV 492
Cdd:cd10276   1 PPTDLPEPTPEFDPEVLWSKSVGNGGMAGIDLTPVVAGDMVYAADANGQ-VSAFNATTGKIIWETSLsgkGFLGGTPAVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 493 GGVVLLTGADARVTALDAATGEEKWRRRIPGQPQPAFVSYGDGLAYAVAAAGsgtKVAAVDPESGATRWQRRFD-GVLSL 571
Cdd:cd10276  80 NGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPTYADGKIYVGTGDG---RLYYCNAETGKVVWNRTSTaPELSL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 572 ------VGAHDGAVWFAST------TADsDTDAVVRYDVTRRTVRRVGLRFPLQGAQAVVRKDTVYVLANGGALVAVDTR 639
Cdd:cd10276 157 rggaapVGAYDVVFVGDGNgtvvalNTG-TGVDIWEFSVSEPRGRTELPRMIDSSVTYVVVGGYLYSTSYQGYLVALDFE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 640 TSKELWRLETSvSFASAPVAAGDRVYFAGADGRLLAVDASKG-------VLLGQTKA----------------------- 689
Cdd:cd10276 236 SGQFLWSRKAS-GGTSTSTDANGRVYVGDGEGSLYCLDASTGdelwsqtVLLGRVLSspaiyvgvyiyvtdnaegylycl 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 29831260 690 -RLGGA------HGSLVSGLPSPVAADGKVYSAAPDGSLFAVD 725
Cdd:cd10276 315 kDNDGLtvarveVDYSQYILQGPAVSDGWLYYGTDDGYLYALT 357
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
64-172 1.09e-10

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


Pssm-ID: 226168  Cd Length: 204  Bit Score: 60.76  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  64 RGRFRQEV---AAARRVsGAFTAPVVDADPGAGRPWMAtlFIPGPTLAEHVKRNgalPPARLRHL--MAGLaealrdIHR 138
Cdd:COG3642  43 RERTRREArilAKAREA-GVPVPIVYDVDPDNGLIVME--YIEGELLKDALEEA---RPDLLREVgrLVGK------LHK 110
                        90       100       110
                ....*....|....*....|....*....|....
gi 29831260 139 AGVVHRDLKPSNVLLAEDGPKVIDFGISRPSDSE 172
Cdd:COG3642 111 AGIVHGDLTTSNIILSGGRIYFIDFGLGEFSDEV 144
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
60-171 8.77e-10

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: 57.61  E-value: 8.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    60 DPEFRGRFRQE--VAAARRVSGAFTA----PVV-DADPGAGRPWMAtlFIPGPTLAEHVKRNGAlpparlrHLMAGLAEA 132
Cdd:TIGR03724  32 HPELDERIRRErtRNEARLLSRARKAgvntPVVyDVDPDNKTIVME--YIEGKPLKDVIEEGND-------ELLREIGRL 102
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 29831260   133 LRDIHRAGVVHRDLKPSNVLLAEDGPKVIDFGISRPSDS 171
Cdd:TIGR03724 103 VGKLHKAGIVHGDLTTSNIIVRDDKLYLIDFGLGKYSDE 141
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
60-171 2.72e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 56.45  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   60 DPEFRGRFRQE--VAAARRVSGAFTA----PVV-DADPGAGRPWMAtlFIPGPTLAEHVKRNGAlppaRLRHLMAGLAEA 132
Cdd:PRK14879  34 HPELDERIRRErtRREARIMSRARKAgvnvPAVyFVDPENFIIVME--YIEGEPLKDLINSNGM----EELELSREIGRL 107
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 29831260  133 LRDIHRAGVVHRDLKPSNVLLAEDGPKVIDFGISRPSDS 171
Cdd:PRK14879 108 VGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLAEFSKD 146
PQQ_3 pfam13570
PQQ-like domain;
642-679 1.41e-05

PQQ-like domain;


Pssm-ID: 257887  Cd Length: 40  Bit Score: 43.37  E-value: 1.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 29831260   642 KELWRLETSVSFASAPVAAGDRVYFAGADGRLLAVDAS 679
Cdd:pfam13570   2 KVLWSFDTGGPVVSSPAVDGGTVYVGSGDGTLYALDAA 39
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
130-278 1.94e-04

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 41.62  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    130 AEALRDIHRAGVVHRDLKPSNVLLAEDGPKVIdfgISRPSDselrtetgklIGTPPFMAPEQFRRpREVGPAADVFALGS 209
Cdd:smart00750  27 LGALRELHRQAKSGNILLTWDGLLKLDGSVAF---KTPEQS----------RPDPYFMAPEVIQG-QSYTEKADIYSLGI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    210 VIVHAATGSGPfDSDSPYLVAY----------QVVHDEPDLTGVPE--ELAELVAGCLAKEPDDRPTPDELMTALRSVSA 277
Cdd:smart00750  93 TLYEALDYELP-YNEERELSAIleillngmpaDDPRDRSNLEGVSAarSFEDFMRLCASRLPQRREAANHYLAHCRALFA 171

                   .
gi 29831260    278 S 278
Cdd:smart00750 172 E 172
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
109-164 1.35e-03

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 250410  Cd Length: 186  Bit Score: 39.13  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29831260   109 EHVKRNGaLPPARLRH--LMAGLAEALRDI--------HRAGVVHRDLKPSNVLLAEDGPKVIDFG 164
Cdd:pfam01163  84 EFIGDDG-VPAPRLKDveLEEEAEEIYDEIiremrrlyQEAGLVHGDLSEYNVLVDDDKPVIIDVP 148
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
23-270 4.68e-50

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.80  E-value: 4.68e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260     23 YLLEAALGSGGMGVVHLARS-ASGLRLAVKVVHAQyaQDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLF 101
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    102 IPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFGISRPSDSELRTETgkL 180
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFGLARQLDPGEKLTT--F 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    181 IGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVV-----HDEPDLTGVPEELAELVAGCL 255
Cdd:smart00220 157 VGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIgkpkpPFPPPEWDISPEAKDLIRKLL 235
                          250
                   ....*....|....*
gi 29831260    256 AKEPDDRPTPDELMT 270
Cdd:smart00220 236 VKDPEKRLTAEEALQ 250
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
422-681 6.34e-29

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 257688 [Multi-domain]  Cd Length: 237  Bit Score: 115.95  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   422 AAVDPADGKVLWSRGDAKRHSDGTVRPPVLSGGLLHVVSEGGkRLAALDPATGKTRWSHDL-AAYGGRFAQVGGVVLLTG 500
Cdd:pfam13360   6 SALDAATGKVLWRVDLGPAAGTALGGGVAVDGGRLYVATGKG-ELVALDAADGKLLWRKDLsGEILGAPLVAGGRVYVVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   501 ADARVTALDAATGEEKWRRRIPGQPQ-----PAFVSYGDglayAVAAAGSGTKVAAVDPESGATRWQRRfdgvlslvgah 575
Cdd:pfam13360  85 ADGSLYALDAKTGKLLWSYQRSLPPLtlrgsSSPAIVGD----TVIVGFSSGKLVALDPKTGKVLWEAP----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   576 dgavwFASTTADSDTDAVVryDVTrrtvrrvglrfplqgAQAVVRKDTVYVLANGGALVAVDTRTSKELWRLEtsVSFAS 655
Cdd:pfam13360 150 -----VARPRGGSEIERLV--DIT---------------GTPVVDGGRVYASSYQGRLVAIDLATGKRLWSRP--ISSVN 205
                         250       260
                  ....*....|....*....|....*.
gi 29831260   656 APVAAGDRVYFAGADGRLLAVDASKG 681
Cdd:pfam13360 206 GPAVDGGVLFVVDDDGELVALDRATG 231
Pkinase pfam00069
Protein kinase domain;
23-269 1.05e-46

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 166.65  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    23 YLLEAALGSGGMGVVHLAR-SASGLRLAVKVVHAQYAqDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLF 101
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKhKGTGKIVAVKILKKRSE-KSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   102 IPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDG-PKVIDFGISRP---SDSELRTET 177
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGvVKIADFGLAKKltkSSSSLTTFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   178 gkliGTPPFMAPEQFRRPREVGPAADVFALGSVIVHAATGSGPFDSDSPY--LVAYQVV------HDEPDLTGVPEELAE 249
Cdd:pfam00069 160 ----GTPEYMAPEVLLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILdqLQLIRRIlgppleFDEPKSDSGSEEAKD 235
                         250       260
                  ....*....|....*....|
gi 29831260   250 LVAGCLAKEPDDRPTPDELM 269
Cdd:pfam00069 236 LIKKCLNKDPSKRPTAEEIL 255
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
23-269 2.23e-38

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: 146.81  E-value: 2.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  23 YLLEAALGSGGMGVVHLARSAsgLRLAVKVVHAQYAQDPEFRGRFRQEVAAARRVSGA-FTAPVVDADPGAGRPWMATLF 101
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 102 IPGPTLAEHVKRNG---ALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDG--PKVIDFGISRP-----SDS 171
Cdd:COG0515  80 VDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrvVKLIDFGLAKLlpdpgSTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 172 ELRTETGKLIGTPPFMAPEQFR--RPREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVV--------------H 235
Cdd:COG0515 160 SIPALPSTSVGTPGYMAPEVLLglSLAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpslaspL 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 29831260 236 DEPDLTGVPEELAELVAGCLAKEPDDRPTPDELM 269
Cdd:COG0515 240 SPSNPELISKAASDLLKKLLAKDPKNRLSSSSDL 273
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
376-684 9.50e-24

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ [Protein fate, Protein and peptide secretion and trafficking].


Pssm-ID: 234163 [Multi-domain]  Cd Length: 377  Bit Score: 102.70  E-value: 9.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   376 QDAAPSKAAFQPWDIGLSAGGSKATGMAQCAYAPHRLYCTRPGVLAAAVDPADGKVLWSRgdakRHSDGTVRPPVLSGGL 455
Cdd:TIGR03300  32 PEFQPTVKVDQVWSASVGDGGGHYYYRLQPAVAGGKVYAADADGTVVALDAETGKRLWRV----DLDERLSGGVGADGGL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   456 LHVVSEGGKrLAALDPATGKTRW-----SHDLAAyggrfAQV-GGVVLLTGADARVTALDAATGEEKWR--RRIP----- 522
Cdd:TIGR03300 108 VFVGTEKGE-VIALDAEDGKELWraklsSEVLSP-----PLVaNGLVVVRTNDGRLTALDAATGERLWTysRVTPaltlr 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   523 GQPQPAFVsygDGLAYAVAAAGsgtKVAAVDPESGATRWQRRfdgvlslVGAHDGAvwfasttadSDTDAVVryDVTrrt 602
Cdd:TIGR03300 182 GSASPVIA---DGGVLVGFAGG---KLVALNLQTGQPLWEQR-------VALPKGR---------TELERLV--DVD--- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   603 vrrvglrfplqgAQAVVRKDTVYVLANGGALVAVDTRTSKELWRLETSVsfASAPVAAGDRVYFAGADGRLLAVDASKGV 682
Cdd:TIGR03300 235 ------------GDPVVDGGQVYAVSYQGRVAALDLRSGRVLWKRDASS--YQGPAVDDNRLYVTDADGVVVALDRRSGS 300

                  ..
gi 29831260   683 LL 684
Cdd:TIGR03300 301 EL 302
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
44-267 1.48e-22

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: 102.23  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260     44 SGLRLAVKVVHAQYAQDPEFRGRFRQEVAAARRVSGAFTAPVVDA-DPGAGRPWMATLFIPGPTLAEHVKRNGALPPARL 122
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    123 RHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDG----PKVIDFGIS------RPSDSELRTETGKLIGTPPFMAPEQF 192
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrphAKVLDFGIGtllpgvRDADVATLTRTTEVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260    193 RRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQvvHDEPDLTGVPE-----ELAELVAGCLAKEPDDRPTPDE 267
Cdd:TIGR03903  162 RG-EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ--QLSPVDVSLPPwiaghPLGQVLRKALNKDPRQRAASAP 238
COG1520 COG1520
FOG: WD40-like repeat [Function unknown]
417-725 1.50e-21

FOG: WD40-like repeat [Function unknown]


Pssm-ID: 224437 [Multi-domain]  Cd Length: 370  Bit Score: 96.10  E-value: 1.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 417 PGVLAAAVDPADGKVLWSRGDAKRHSDGTVRP-PVLSGGLLHVVSEGGKrLAALDPATGKTRWSHDL----AAYGGRFAQ 491
Cdd:COG1520  31 GADLVAVANNTSGTLLWSVSLGSGGGGIYAGPaPADGDGTVYVGTRDGN-IFALNPDTGLVKWSYPLlgavAQLSGPILG 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 492 VGGVVLLTGADARVTALDAATGEEKWRRRIPGqpQPAFVS---YGDGLAYAVAAAGsgtKVAAVDPESGATRWQRRFDGV 568
Cdd:COG1520 110 SDGKIYVGSWDGKLYALDASTGTLVWSRNVGG--SPYYASppvVGDGTVYVGTDDG---HLYALNADTGTLKWTYETPAP 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 569 LSL-----VGAHDGAVWFASTTADSDTDAVVRYDVTRRTVRRVGL--------RFPLQGAQAVVRKDTVYVLANGGALVA 635
Cdd:COG1520 185 LSLsiygsPAIASGTVYVGSDGYDGILYALNAEDGTLKWSQKVSQtigrtaisTTPAVDGGPVYVDGGVYAGSYGGKLLC 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 636 VDTRTSKELWRLETSVSFASAP-----VAAGD-RVYF------AGADGRLLAVDASKGVLLGQTKARLGGAhgslvSGLP 703
Cdd:COG1520 265 LDADTGELIWSFPAGGSVQGSGlyttpVAGADgKVYIgftdndGRGSGSLYALADVPGGTLLKWSYPVGGG-----YSLS 339
                       330       340
                ....*....|....*....|...
gi 29831260 704 SPVAADGKVYSA-APDGSLFAVD 725
Cdd:COG1520 340 TVAGSDGTLYFGgDDGRGLYAFR 362
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
416-724 1.19e-16

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857 [Multi-domain]  Cd Length: 394  Bit Score: 81.13  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  416 RPGVLAAaVDPADGKVLWSRGDAKRHS-DGTVRPPVLSGGL------LHVVSEGGKrLAALDPATGKTRWShdlaayggr 488
Cdd:PRK11138  77 RAGLVKA-LDADTGKEIWSVDLSEKDGwFSKNKSALLSGGVtvaggkVYIGSEKGQ-VYALNAEDGEVAWQ--------- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  489 fAQVGG-----------VVLLTGADARVTALDAATGEEKWR--RRIP-----GQPQPAfVSYGdglayAVAAAGSGTKVA 550
Cdd:PRK11138 146 -TKVAGealsrpvvsdgLVLVHTSNGMLQALNESDGAVKWTvnLDVPsltlrGESAPA-TAFG-----GAIVGGDNGRVS 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  551 AVDPESGATRWQRRfdgvlslVGAHDGAVWFaSTTADSDTDAVVrydvtrrtvrrVGlrfplqgaqavvrkDTVYVLANG 630
Cdd:PRK11138 219 AVLMEQGQLIWQQR-------ISQPTGATEI-DRLVDVDTTPVV-----------VG--------------GVVYALAYN 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  631 GALVAVDTRTSKELWRLETSvSFASAPVaAGDRVYFAGADGRLLAVDASKGVLL---GQTKARL---------------- 691
Cdd:PRK11138 266 GNLVALDLRSGQIVWKREYG-SVNDFAV-DGGRIYLVDQNDRVYALDTRGGVELwsqSDLLHRLltapvlyngylvvgds 343
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 29831260  692 -GGAH------GSLV-------SGLPS-PVAADGKVYSAAPDGSLFAV 724
Cdd:PRK11138 344 eGYLHwinredGRFVaqqkvdsSGFLSePVVADDKLLIQARDGTVYAI 391
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
13-269 1.45e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 78.76  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   13 EAEHPQYAGQYLLEAALGSGGMGVVHLARSAS-GLRLAVKVVHAQyAQDPEFRGRFRQEVA------------------- 72
Cdd:PTZ00283  24 EATAKEQAKKYWISRVLGSGATGTVLCAKRVSdGEPFAVKVVDME-GMSEADKNRAQAEVCcllncdffsivkchedfak 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   73 --AARRVSGAFTAPVVD-ADPGAGRPWMATLFIPGPTLAEHvkrngalpPARLRHLMAGLAeaLRDIHRAGVVHRDLKPS 149
Cdd:PTZ00283 103 kdPRNPENVLMIALVLDyANAGDLRQEIKSRAKTNRTFREH--------EAGLLFIQVLLA--VHHVHSKHMIHRDIKSA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  150 NVLLAEDG-PKVIDFGISRPSDSELRTETGK-LIGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPY 227
Cdd:PTZ00283 173 NILLCSNGlVKLGDFGFSKMYAATVSDDVGRtFCGTPYYVAPEIWRR-KPYSKKADMFSLGVLLYELLTLKRPFDGENME 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 29831260  228 LVAYQVVHD--EPDLTGVPEELAELVAGCLAKEPDDRPTPDELM 269
Cdd:PTZ00283 252 EVMHKTLAGryDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLL 295
pknD PRK13184
serine/threonine-protein kinase; Reviewed
21-274 5.66e-14

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 74.42  E-value: 5.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   21 GQYLLEAALGSGGMGVVHLARS-ASGLRLAVKVVHAQYAQDPEFRGRFRQEVAAARRVSGAFTAPVV----DADPgagrP 95
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDpVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYsicsDGDP----V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   96 WMATLFIPGPTLA---EHVKRNGALP---------PARLRhLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGPKVI-- 161
Cdd:PRK13184  78 YYTMPYIEGYTLKsllKSVWQKESLSkelaektsvGAFLS-IFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVIld 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  162 -----------------DFGISRPSDSELrTETGKLIGTPPFMAPEQFrRPREVGPAADVFALGSVIVHAATGSGPF-DS 223
Cdd:PRK13184 157 wgaaifkkleeedlldiDVDERNICYSSM-TIPGKIVGTPDYMAPERL-LGVPASESTDIYALGVILYQMLTLSFPYrRK 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 29831260  224 DSPYLVAYQVVHDEPDLT---GVPEELAELVAGCLAKEPDDR-PTPDELMTALRS 274
Cdd:PRK13184 235 KGRKISYRDVILSPIEVApyrEIPPFLSQIAMKALAVDPAERySSVQELKQDLEP 289
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
29-269 3.59e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 60.99  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   29 LGSGGMGVVHLARSASGLRL-AVKVVHAQYaqDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLFIPGPTL 107
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLyALKVIYGNH--EDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  108 -AEHVKRNGALPPARlRHLMAGLAEalrdIHRAGVVHRDLKPSNVLL-AEDGPKVIDFGISR-------PSDSElrtetg 178
Cdd:PLN00034 160 eGTHIADEQFLADVA-RQILSGIAY----LHRRHIVHRDIKPSNLLInSAKNVKIADFGVSRilaqtmdPCNSS------ 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  179 klIGTPPFMAPEQ----FRRPREVGPAADVFALGSVIVHAATGSGPF----DSDSPYLVAYQVVHDEPDL-TGVPEELAE 249
Cdd:PLN00034 229 --VGTIAYMSPERintdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAICMSQPPEApATASREFRH 306
                        250       260
                 ....*....|....*....|
gi 29831260  250 LVAGCLAKEPDDRPTPDELM 269
Cdd:PLN00034 307 FISCCLQREPAKRWSAMQLL 326
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
101-224 3.79e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 56.79  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  101 FIPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLL--AEDGPKVIDFGISRPSDSElrtetG 178
Cdd:PHA03390  90 YIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYdrAKDRIYLCDYGLCKIIGTP-----S 164
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 29831260  179 KLIGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSD 224
Cdd:PHA03390 165 CYDGTLDYFSPEKIKG-HNYDVSFDWWAVGVLTYELLTGKHPFKED 209
PQQ_enz_alc_DH TIGR03075
PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic ...
613-712 3.25e-08

PQQ-dependent dehydrogenase, methanol/ethanol family; This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see pfam01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens.


Pssm-ID: 234102 [Multi-domain]  Cd Length: 526  Bit Score: 55.38  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260   613 QGAQAVVRKDTVYVLANGGALVAVDTRTSKELWRLETSVSFASAPVA-----------AGDRVYFAGADGRLLAVDASKG 681
Cdd:TIGR03075  61 QESQPLVVDGVMYVTTSYSRVYALDAKTGKELWKYDPKLPDDIIPVMccdvvnrgaalYDGKVFFGTLDARLVALDAKTG 140
                          90       100       110
                  ....*....|....*....|....*....|.
gi 29831260   682 VLLGQTKArLGGAHGSLVSGLPSPVaaDGKV 712
Cdd:TIGR03075 141 KVVWSKKN-GDYKKGYTITAAPLVV--KGKV 168
COG1520 COG1520
FOG: WD40-like repeat [Function unknown]
601-728 2.81e-07

FOG: WD40-like repeat [Function unknown]


Pssm-ID: 224437 [Multi-domain]  Cd Length: 370  Bit Score: 51.81  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 601 RTVRRVGLRFPLQGAQAVVRKDTVYVLANGGALVAVDTRTS-KELWRLE----TSVSFAS-APVAAGDRVYFAGADGRLL 674
Cdd:COG1520   2 STLSLLGRLFATLGATPVLAAGTDYLVAVGADLVAVANNTSgTLLWSVSlgsgGGGIYAGpAPADGDGTVYVGTRDGNIF 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 29831260 675 AVDASKGVLLGQTKarLGGAHGSLVSGlpsPVAADGKVYSAAPDGSLFAVDARR 728
Cdd:COG1520  82 ALNPDTGLVKWSYP--LLGAVAQLSGP---ILGSDGKIYVGSWDGKLYALDAST 130
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
29-269 3.01e-41

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 150.08  E-value: 3.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLARS-ASGLRLAVKVVHAQyaQDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLFIPGPTL 107
Cdd:cd00180   1 LGEGGFGTVYLARDkKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 108 AEHVKRNGA-LPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP--KVIDFGISRPSDSElRTETGKLIGTP 184
Cdd:cd00180  79 KDLLKENEGkLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGkvKLADFGLSKLLTSD-KSLLKTIVGTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 185 PFMAPEQFRRPREVGPAADVFALGsvivhaatgsgpfdsdspyLVAYQVvhdepdltgvpEELAELVAGCLAKEPDDRPT 264
Cdd:cd00180 158 AYMAPEVLLGKGYYSEKSDIWSLG-------------------VILYEL-----------PELKDLIRKMLQKDPEKRPS 207

                ....*
gi 29831260 265 PDELM 269
Cdd:cd00180 208 AKEIL 212
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
29-268 1.52e-37

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: 141.16  E-value: 1.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLARS-ASGLRLAVKVVHAQYaQDPEFRGRFRQEVAAARRVS--------GAFTAPVVDadpgagrpwMAT 99
Cdd:cd06606   8 LGRGSFGSVYLALDkDTGELMAVKSVELSG-DSEEELEALEREIRILSSLQhpnivryyGSERDEEKN---------TLN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 100 LF---IPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFGISRP-SDSELR 174
Cdd:cd06606  78 IFleyVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVvKLADFGCAKRlGDIETG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 175 TETGKLIGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPF-DSDSPYLVAYQVVHDE--PDL-TGVPEELAEL 250
Cdd:cd06606 158 EGTGSVRGTPYWMAPEVIRG-EEYGRAADIWSLGCTVIEMATGKPPWsELGNPMAALYKIGSSGepPEIpEHLSEEAKDF 236
                       250
                ....*....|....*...
gi 29831260 251 VAGCLAKEPDDRPTPDEL 268
Cdd:cd06606 237 LRKCLRRDPKKRPTADEL 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
29-269 3.51e-30

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: 120.00  E-value: 3.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLARS-ASGLRLAVKVVHAQYAQDPEFRGRfrqEVAAARRVS--------GAFTAPvvdadpgaGRPWMAT 99
Cdd:cd05122   8 IGKGGFGEVYKARHkRTGKEVAIKVIKLESKEKKEKIIN---EIQILKKCKhpnivkyyGSYLKK--------DELWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 100 LFIPGPTLAEHVK-RNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFGIS-RPSDSELRTE 176
Cdd:cd05122  77 EFCSGGSLKDLLKsTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEvKLIDFGLSaQLSDTKARNT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 177 TgklIGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVVHDEP----DLTGVPEELAELVA 252
Cdd:cd05122 157 M---VGTPYWMAPEVING-KPYDYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATNGPpglrNPEKWSDEFKDFLK 232
                       250
                ....*....|....*..
gi 29831260 253 GCLAKEPDDRPTPDELM 269
Cdd:cd05122 233 KCLQKNPEKRPTAEQLL 249
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
29-270 2.68e-28

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: 114.61  E-value: 2.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLAR-SASGLRLAVKVVHaqYAQDPEFRGRFRQEVAAARRVS--------GAFtapvvdADPGAGRPWMAt 99
Cdd:cd06623   9 LGQGSSGVVYKVRhKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRSCEspyvvkcyGAF------YKEGEISIVLE- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 100 lFIPGPTLAEHVKRNGALPPARL----RHLMAGLAeALRDIHRagVVHRDLKPSNVLLAEDG-PKVIDFGISRPSDSELr 174
Cdd:cd06623  80 -YMDGGSLADLLKKVGKIPEPVLayiaRQILKGLD-YLHTKRH--IIHRDIKPSNLLINSKGeVKIADFGISKVLENTL- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 175 TETGKLIGTPPFMAPEQFRrPREVGPAADVFALGSVIVHAATGSGPFDSD---SPYLVAYQVVHDE-PDL--TGVPEELA 248
Cdd:cd06623 155 DQCNTFVGTVTYMSPERIQ-GESYSYAADIWSLGLTLLECALGKFPFLPPgqpSFFELMQAICDGPpPSLpaEEFSPEFR 233
                       250       260
                ....*....|....*....|..
gi 29831260 249 ELVAGCLAKEPDDRPTPDELMT 270
Cdd:cd06623 234 DFISACLQKDPKKRPSAAELLQ 255
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
101-262 5.32e-28

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: 113.38  E-value: 5.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 101 FIPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFGISRPSDSELRTeTGK 179
Cdd:cd05123  74 YAPGGELFSHLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHiKLTDFGLAKELSSEGSR-TNT 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 180 LIGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVVHDEPDL-TGVPEELAELVAGCLAKE 258
Cdd:cd05123 153 FCGTPEYLAPEVLLG-KGYGKAVDWWSLGVLLYEMLTGKPPFYAEDRKEIYEKILKDPLRFpEFLSPEARDLISGLLQKD 231

                ....
gi 29831260 259 PDDR 262
Cdd:cd05123 232 PTKR 235
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
22-268 8.11e-28

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: 113.36  E-value: 8.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  22 QYLLEAALGSGGMGVVHLARS-ASGLRLAVKVVHAQyAQDPEFRGRFRQEVAAARRVS--------GAFtapvVDADpga 92
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRkSDGKLYVLKEIDLS-NMSEKEREDALNEVKILKKLNhpniikyyESF----EEKG--- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  93 grpwmaTLFI-----PGPTLAEHVKR----NGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVID 162
Cdd:cd08215  73 ------KLCIvmeyaDGGDLSQKIKKqkkeGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLvKLGD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 163 FGISRP-SDSELRTETgkLIGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVVHDE--PD 239
Cdd:cd08215 147 FGISKVlSSTVDLAKT--VVGTPYYLSPELCQN-KPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQypPI 223
                       250       260
                ....*....|....*....|....*....
gi 29831260 240 LTGVPEELAELVAGCLAKEPDDRPTPDEL 268
Cdd:cd08215 224 PSQYSSELRNLVSSLLQKDPEERPSIAQI 252
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
101-274 4.93e-27

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: 111.52  E-value: 4.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 101 FIPGPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFGISRPSDSELRTETGK 179
Cdd:cd05581  83 YAPNGELLQYIRKYGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILLDKDMHiKITDFGTAKVLDPNSSPESNK 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 180 L-------------------IGTPPFMAPEQFRRpREVGPAADVFALGSVIVHAATGSGPFDSDSPYLVAYQVVHDEPDL 240
Cdd:cd05581 163 GdatnidsqieknrrrfasfVGTAEYVSPELLNE-KPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKILKLEYSF 241
                       170       180       190
                ....*....|....*....|....*....|....*
gi 29831260 241 T-GVPEELAELVAGCLAKEPDDRPTPDELMTALRS 274
Cdd:cd05581 242 PpNFPPDAKDLIEKLLVLDPQDRLGVNEGYDELKA 276
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
104-270 1.32e-23

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: 100.88  E-value: 1.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 104 GPTLAEHVKRNGALPPARLRHLMAGLAEALRDIHRAGVVHRDLKPSNVLLAEDGP-KVIDFG----ISRPSDSeLRTETG 178
Cdd:cd06626  83 GGTLEELLEHGRILDEHVIRVYTLQLLEGLAYLHSHGIVHRDIKPANIFLDHNGViKLGDFGcavkLKNNTTT-MGEEVQ 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 179 KLIGTPPFMAPEQFRRPREVGP--AADVFALGSVIVHAATGSGPFDS-DSPYLVAYQVVHDE----PDLTGVPEELAELV 251
Cdd:cd06626 162 SLAGTPAYMAPEVITGGKGKGHgrAADIWSLGCVVLEMATGKRPWSElDNEFQIMFHVGAGHkppiPDSLQLSPEGKDFL 241
                       170
                ....*....|....*....
gi 29831260 252 AGCLAKEPDDRPTPDELMT 270
Cdd:cd06626 242 DRCLESDPKKRPTASELLQ 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
29-270 7.53e-23

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 98.54  E-value: 7.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  29 LGSGGMGVVHLAR-SASGLRLAVKVVHAqyAQDPEFRGRFRQEVAAARRVSGAFTAPVVDADPGAGRPWMATLFIPGPTL 107
Cdd:cd06605   9 LGAGNSGVVSKVLhRPTGKIMAVKTIRL--EINEAIQKQILRELDILHKCNSPYIVGFYGAFYNNGDISICMEYMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 108 AEHVKR-NGALPPARLRHLMAGLAEALRDIHRA-GVVHRDLKPSNVLLAEDGP-KVIDFGISRpsdsELRTETGK-LIGT 183
Cdd:cd06605  87 DKILKEvQGRIPERILGKIAVAVLKGLTYLHEKhKIIHRDVKPSNILVNSRGQiKLCDFGVSG----QLVNSLAKtFVGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 184 PPFMAPEQFrRPREVGPAADVFALGSVIVHAATGSGPFDS-DSPY-----LVAYQVVHDEPDLTG--VPEELAELVAGCL 255
Cdd:cd06605 163 SSYMAPERI-QGNDYSVKSDIWSLGLSLIELATGRFPYPPeNDPPdgifeLLQYIVNEPPPRLPSgkFSPDFQDFVNLCL 241
                       250
                ....*....|....*
gi 29831260 256 AKEPDDRPTPDELMT 270
Cdd:cd06605 242 IKDPRERPSYKELLE 256
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
416-725 1.65e-22

Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.


Pssm-ID: 199834 [Multi-domain]  Cd Length: 358  Bit Score: 98.56  E-value: 1.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 416 RPGVLAAAVDPADGKVLWSRGDAKRHSDGTVRPPVLSGGLLHVVSEGGKrLAALDPATGKTRWSHDL---AAYGGRFAQV 492
Cdd:cd10276   1 PPTDLPEPTPEFDPEVLWSKSVGNGGMAGIDLTPVVAGDMVYAADANGQ-VSAFNATTGKIIWETSLsgkGFLGGTPAVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 493 GGVVLLTGADARVTALDAATGEEKWRRRIPGQPQPAFVSYGDGLAYAVAAAGsgtKVAAVDPESGATRWQRRFD-GVLSL 571
Cdd:cd10276  80 NGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSPPTYADGKIYVGTGDG---RLYYCNAETGKVVWNRTSTaPELSL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 572 ------VGAHDGAVWFAST------TADsDTDAVVRYDVTRRTVRRVGLRFPLQGAQAVVRKDTVYVLANGGALVAVDTR 639
Cdd:cd10276 157 rggaapVGAYDVVFVGDGNgtvvalNTG-TGVDIWEFSVSEPRGRTELPRMIDSSVTYVVVGGYLYSTSYQGYLVALDFE 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260 640 TSKELWRLETSvSFASAPVAAGDRVYFAGADGRLLAVDASKG-------VLLGQTKA----------------------- 689
Cdd:cd10276 236 SGQFLWSRKAS-GGTSTSTDANGRVYVGDGEGSLYCLDASTGdelwsqtVLLGRVLSspaiyvgvyiyvtdnaegylycl 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 29831260 690 -RLGGA------HGSLVSGLPSPVAADGKVYSAAPDGSLFAVD 725
Cdd:cd10276 315 kDNDGLtvarveVDYSQYILQGPAVSDGWLYYGTDDGYLYALT 357
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
22-269 1.71e-22

Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; Serine/threonine kinases (STKs), oxidative stress response kinase (OSR1) and Ste20-related proline alanine-rich kinase (SPAK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The OSR1 and SPAK 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. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates.


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 97.81  E-value: 1.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29831260  22 QYLLEAALGSGGMGVVHLARSAS-GLRLAVKVVHAQyaQDPEFRGRFRQEVAAAR-----RVSGAFTAPVVDADPgagrp 95
Cdd:cd06610   2 D