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Conserved domains on  [gi|37520665|ref|NP_924042|]
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serine/threonine protein kinase [Gloeobacter violaceus PCC 7421]

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
80-341 5.93e-75

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


:

Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 247.50  E-value: 5.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  80 PYRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAELG-TETLVRRFRLERQILADLDHPNIAHLIDGGTTaGGLPYL 158
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAeDEEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 159 VMDYIDGEPIDRYC-ERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEhaesia 237
Cdd:cd14014  78 VMEYVEGGSLADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG------ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 238 pEASLTvgteqPAGVTGGalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGsRPPRPG--------------PEPAA 303
Cdd:cd14014 152 -DSGLT-----QTGSVLG--TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTG-RPPFDGdspaavlakhlqeaPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 37520665 304 RPQSSQLEELDSIACKAMSVEPEGRYPSVDAFAADIRN 341
Cdd:cd14014 223 PLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TolB_N super family cl21526
TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent ...
399-521 5.69e-31

TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent translocation system. This function of this amino terminal domain is uncertain.


The actual alignment was detected with superfamily member COG5616:

Pssm-ID: 276345  Cd Length: 152  Bit Score: 120.15  E-value: 5.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 399 TVVVLPFSERGSTGD-ERLADGLTLSLTTHLGKVAALTVISDRAAMQYRDSS--LAQIGGDLGATGVLTGSVLRSGERVR 475
Cdd:COG5616  26 SIAVLPFVNLSGDPEqEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAvdVREVGEELGVRYVLEGSVRRAGGRVR 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37520665 476 IAARLVDPRSGTQLWAEQYDRKLQDIFAIQTEVAQRIAAAMKAKLT 521
Cdd:COG5616 106 VTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYG 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
494-781 1.76e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 52.54  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 494 YDRKLQDIFAIQTEVAQRIAAAMKAKLTPEEKIRLARAPAQNAMAYQYYLRGREYNNRFTVKDNEYAIGFFKQALALDPD 573
Cdd:COG0457  12 LEALAKLLAEALALLEAGLALLELLGELAEALELLEEALELLPNSDLAGLLLLLALALLKLGRLEEALELLEKALELELL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 574 FALARSGLAVGYLNRFIyggKVSWREAACREAGRAVALESGLAEAHNAMAACYSQMELRlqpQAMAEYRRAIDLNP---N 650
Cdd:COG0457  92 PNLAEALLNLGLLLEAL---GKYEEALELLEKALALDPDPDLAEALLALGALYELGDYE---EALELYEKALELDPelnE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 651 FFSAMYNYSAILASLGRLDEGLYWMKKAVRVNP-LCIGCYRSIASYYWLLGEAAKGDVWIDKGLALIPDGARLHVSRGRA 729
Cdd:COG0457 166 LAEALLALGALLEALGRYEEALELLEKALKLNPdDDAEALLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYNLALL 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 37520665 730 YLPRGRYDEARQIALQVLKEEPNnaealsLAGTAERLSGRWERSRRYYERML 781
Cdd:COG0457 246 LLELGRYEEALEALEKALELDPD------LYNLGLALLLLLAEALELLEKAD 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
81-298 8.35e-48

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 171.17  E-value: 8.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665     81 YRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAELGTEtLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLVM 160
Cdd:smart00220   1 YEILEKLGEGSFGKVYLAR--DKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665    161 DYIDGEPI-DRYCERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEHAESIAPe 239
Cdd:smart00220  77 EYCEGGDLfDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT- 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 37520665    240 aslTVGteqpagvtggalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGsRPPRPG 298
Cdd:smart00220 156 ---FVG------------TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTG-KPPFPG 198
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
80-341 5.93e-75

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 247.50  E-value: 5.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  80 PYRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAELG-TETLVRRFRLERQILADLDHPNIAHLIDGGTTaGGLPYL 158
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAeDEEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 159 VMDYIDGEPIDRYC-ERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEhaesia 237
Cdd:cd14014  78 VMEYVEGGSLADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG------ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 238 pEASLTvgteqPAGVTGGalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGsRPPRPG--------------PEPAA 303
Cdd:cd14014 152 -DSGLT-----QTGSVLG--TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTG-RPPFDGdspaavlakhlqeaPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 37520665 304 RPQSSQLEELDSIACKAMSVEPEGRYPSVDAFAADIRN 341
Cdd:cd14014 223 PLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
TolBN COG5616
TolB amino-terminal domain (function unknown) [General function prediction only];
399-521 5.69e-31

TolB amino-terminal domain (function unknown) [General function prediction only];


Pssm-ID: 227903  Cd Length: 152  Bit Score: 120.15  E-value: 5.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 399 TVVVLPFSERGSTGD-ERLADGLTLSLTTHLGKVAALTVISDRAAMQYRDSS--LAQIGGDLGATGVLTGSVLRSGERVR 475
Cdd:COG5616  26 SIAVLPFVNLSGDPEqEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAvdVREVGEELGVRYVLEGSVRRAGGRVR 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37520665 476 IAARLVDPRSGTQLWAEQYDRKLQDIFAIQTEVAQRIAAAMKAKLT 521
Cdd:COG5616 106 VTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYG 151
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
158-237 1.88e-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: 274749  Cd Length: 199  Bit Score: 39.12  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   158 LVMDYIDGEPIDRYCErrrlavrarlELFLGVCGAVSYA----HQRRIVHRDLKPGNILVTAEGmPRLLDFGVAKLLEHA 233
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIE----------ENGDELAREIGRLvgklHKAGIVHGDLTTSNIIVRDDK-VYLIDFGLGKYSDEI 142

                  ....
gi 37520665   234 ESIA 237
Cdd:TIGR03724 143 EDKA 146
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
494-781 1.76e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 52.54  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 494 YDRKLQDIFAIQTEVAQRIAAAMKAKLTPEEKIRLARAPAQNAMAYQYYLRGREYNNRFTVKDNEYAIGFFKQALALDPD 573
Cdd:COG0457  12 LEALAKLLAEALALLEAGLALLELLGELAEALELLEEALELLPNSDLAGLLLLLALALLKLGRLEEALELLEKALELELL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 574 FALARSGLAVGYLNRFIyggKVSWREAACREAGRAVALESGLAEAHNAMAACYSQMELRlqpQAMAEYRRAIDLNP---N 650
Cdd:COG0457  92 PNLAEALLNLGLLLEAL---GKYEEALELLEKALALDPDPDLAEALLALGALYELGDYE---EALELYEKALELDPelnE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 651 FFSAMYNYSAILASLGRLDEGLYWMKKAVRVNP-LCIGCYRSIASYYWLLGEAAKGDVWIDKGLALIPDGARLHVSRGRA 729
Cdd:COG0457 166 LAEALLALGALLEALGRYEEALELLEKALKLNPdDDAEALLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYNLALL 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 37520665 730 YLPRGRYDEARQIALQVLKEEPNnaealsLAGTAERLSGRWERSRRYYERML 781
Cdd:COG0457 246 LLELGRYEEALEALEKALELDPD------LYNLGLALLLLLAEALELLEKAD 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
81-298 8.35e-48

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 171.17  E-value: 8.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665     81 YRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAELGTEtLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLVM 160
Cdd:smart00220   1 YEILEKLGEGSFGKVYLAR--DKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDKL-YLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665    161 DYIDGEPI-DRYCERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEHAESIAPe 239
Cdd:smart00220  77 EYCEGGDLfDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTT- 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 37520665    240 aslTVGteqpagvtggalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGsRPPRPG 298
Cdd:smart00220 156 ---FVG------------TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTG-KPPFPG 198
Pkinase pfam00069
Protein kinase domain;
81-302 3.12e-43

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 158.56  E-value: 3.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665    81 YRVVGKLGQGGMGSVYLAERADaqYSKQVAIKVLRAELGTETLVRRFRLERQILADLDHPNIAHLIDGGTTaGGLPYLVM 160
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKG--TGKIVAVKILKKRSEKSKKDQTARREIRILRRLSHPNIVRLIDAFED-KDHLYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   161 DYIDGEPIDRYCERRRL-AVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLlehaesiape 239
Cdd:pfam00069  78 EYCEGGDLFDYLSRGGPlSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKK---------- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37520665   240 asLTVGTEQPAGVTGgalTPEYAAPEQLHGG-AITPITDIYALGVVLYELLHGsRPPRPGPEPA 302
Cdd:pfam00069 148 --LTKSSSSLTTFVG---TPEYMAPEVLLGGnGYGPKVDVWSLGVILYELLTG-KPPFSGESIL 205
pknD PRK13184
serine/threonine-protein kinase; Reviewed
78-347 7.21e-42

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 164.56  E-value: 7.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   78 LGPYRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAEL-GTETLVRRFRLERQILADLDHPNIAHlIDGGTTAGGLP 156
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAY--DPVCSRRVALKKIREDLsENPLLKKRFLREAKIAADLIHPGIVP-VYSICSDGDPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  157 YLVMDYIDGEPID------RYCERRRLAVRARLE------LFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDF 224
Cdd:PRK13184  78 YYTMPYIEGYTLKsllksvWQKESLSKELAEKTSvgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  225 GVAKLLEHAE------SIAPEASLTVGTEQPAGVTGgalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGSRPPR-- 296
Cdd:PRK13184 158 GAAIFKKLEEedlldiDVDERNICYSSMTIPGKIVG---TPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRrk 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37520665  297 -----------PGPEPAArPQSSQLEELDSIACKAMSVEPEGRYPSVDAFAADIRNYLDGRP 347
Cdd:PRK13184 235 kgrkisyrdviLSPIEVA-PYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGSP 295
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
81-341 1.06e-40

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 154.90  E-value: 1.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  81 YRVVGKLGQGGMGSVYLAERadaqySKQVAIKVLRAEL-GTETLVRRFRLERQILADLDHP-NIAHLIDGGTTAGGLpYL 158
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD-----RKLVALKVLAKKLeSKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSL-YL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 159 VMDYIDGEPIDRYCERRRLAVRARLELFLG----VCGAVSYAHQRRIVHRDLKPGNILVTAEGM-PRLLDFGVAKLLEHA 233
Cdd:COG0515  76 VMEYVDGGSLEDLLKKIGRKGPLSESEALFilaqILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDFGLAKLLPDP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 234 ESIAPEASLTvgteqpAGVTGgalTPEYAAPEQLHG---GAITPITDIYALGVVLYELLHGSRP---------------- 294
Cdd:COG0515 156 GSTSSIPALP------STSVG---TPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPfegeknssatsqtlki 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 37520665 295 ------PRPGPEPAARPQSSQLEELDSIACKAMSVEPEGRYPSVDAFAADIRN 341
Cdd:COG0515 227 ilelptPSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA 279
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
104-340 2.08e-27

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: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 118.79  E-value: 2.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665    104 QYSKQVAIKVLRAELGT-ETLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLPYLVMDYIDGEPI-DRYCERRRLAVRA 181
Cdd:TIGR03903    1 MTGHEVAIKLLRTDAPEeEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFEYVPGRTLrEVLAADGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665    182 RLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPR---LLDFGVAKLLEHAESIApEASLTVGTEqpagVTGgalT 258
Cdd:TIGR03903   81 TGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPhakVLDFGIGTLLPGVRDAD-VATLTRTTE----VLG---T 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665    259 PEYAAPEQLHGGAITPITDIYALGVVLYELLHGSRP-----------PRPGPEPAARPQSSQLEELDSIACKAMSVEPEG 327
Cdd:TIGR03903  153 PTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVvqgasvaeilyQQLSPVDVSLPPWIAGHPLGQVLRKALNKDPRQ 232
                          250
                   ....*....|...
gi 37520665    328 RYPSVDAFAADIR 340
Cdd:TIGR03903  233 RAASAPALAERFR 245
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
556-866 2.98e-15

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 78.97  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   556 DNEYAIGFFKQALALDPDFALARSGLAVGYLNRfiyggkvswreaacREAGRAVA-LESGLAE------AHNAMAACYS- 627
Cdd:TIGR02917 412 DPSEAIADLETAAQLDPELGRADLLLILSYLRS--------------GQFDKALAaAKKLEKKqpdnasLHNLLGAIYLg 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   628 -----------QMELRLQPQ--------------------AMAEYRRAIDLNPNFFSAMYNYSAILASLGRLDEGLYWMK 676
Cdd:TIGR02917 478 kgdlakareafEKALSIEPDffpaaanlaridiqegnpddAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLE 557
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   677 KAVRVNPLCIGCYRSIASYYWLLGEAAKGDVWIDKGLALIPDGARLHVSRGRAYLPRGRYDEARQIALQVLKEEPNNAEA 756
Cdd:TIGR02917 558 KAAELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALA 637
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665   757 LSLAGTAERLSGRWERSRRYYERMLKLTETTDledagdtslRARTALGYLALQENQPQRAHRlLAQSLDFDRKRIAEGN- 835
Cdd:TIGR02917 638 LLLLADAYAVMKNYAKAITSLKRALELKPDNT---------EAQIGLAQLLLAAKRTESAKK-IAKSLQKQHPKAALGFe 707
                         330       340       350
                  ....*....|....*....|....*....|..
gi 37520665   836 -EEWLYFRDmavihalgGEREAAVVQLREAIK 866
Cdd:TIGR02917 708 lEGDLYLRQ--------KDYPAAIQAYRKALK 731
PilF COG3063
Tfp pilus assembly protein PilF [Cell motility, Extracellular structures];
700-830 1.20e-04

Tfp pilus assembly protein PilF [Cell motility, Extracellular structures];


Pssm-ID: 225605 [Multi-domain]  Cd Length: 250  Bit Score: 43.57  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 700 GEAAKGDVWIDKGLALIPDGARLHVSRGRAYLPRGRYDEARQIALQVLKEEPNNAEALSLAGTAERLSGRWERSRRYYER 779
Cdd:COG3063  49 GDYAQAKKNLEKALEHDPSYYLAHLVRAHYYQKLGENDLADESYRKALSLAPNNGDVLNNYGAFLCAQGRPEEAMQQFER 128
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 37520665 780 MLKLTettdleDAGDTSlRARTALGYLALQENQPQRAHRLLAQSLDFDRKR 830
Cdd:COG3063 129 ALADP------AYGEPS-DTLENLGLCALKAGQFDQAEEYLKRALELDPQF 172
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
80-341 5.93e-75

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB 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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 247.50  E-value: 5.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  80 PYRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAELG-TETLVRRFRLERQILADLDHPNIAHLIDGGTTaGGLPYL 158
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRAR--DTLLGRPVAIKVLRPELAeDEEFRERFLREARALARLSHPNIVRVYDVGED-DGRPYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 159 VMDYIDGEPIDRYC-ERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEhaesia 237
Cdd:cd14014  78 VMEYVEGGSLADLLrERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALG------ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 238 pEASLTvgteqPAGVTGGalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGsRPPRPG--------------PEPAA 303
Cdd:cd14014 152 -DSGLT-----QTGSVLG--TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTG-RPPFDGdspaavlakhlqeaPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 37520665 304 RPQSSQLEELDSIACKAMSVEPEGRYPSVDAFAADIRN 341
Cdd:cd14014 223 PLNPDVPPALDAIILRALAKDPEERPQSAAELLAALRA 260
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
87-288 2.83e-39

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation 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 more than 500 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. 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.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 145.88  E-value: 2.83e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  87 LGQGGMGSVYLAERADAQysKQVAIKVLRAElGTETLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLVMDYIDGE 166
Cdd:cd00180   1 LGKGSFGKVYKARDKETG--KKVAVKVIPKE-KLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFL-YLVMEYCEGG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 167 PI-DRYCERRRL-AVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEHaesiapeasltv 244
Cdd:cd00180  77 SLkDLLKENKGPlSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDS------------ 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 37520665 245 gTEQPAGVTGGALTPEYAAPEQLHGGAITPITDIYALGVVLYEL 288
Cdd:cd00180 145 -DDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
81-294 5.79e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 137.59  E-value: 5.79e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  81 YRVVGKLGQGGMGSVYLAERADAQysKQVAIKVLRAELGTETLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLVM 160
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDG--KLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKL-CIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 161 DYIDGEPIDRYCERRRLAVRARLE-----LFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEHAES 235
Cdd:cd08215  79 EYADGGDLAQKIKKQKKKGQPFPEeqildWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 37520665 236 IapeASLTVGteqpagvtggalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGSRP 294
Cdd:cd08215 159 L---AKTVVG------------TPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHP 202
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
80-294 2.49e-34

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 132.64  E-value: 2.49e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  80 PYRVVGKLGQGGMGSVYLAEraDAQYSKQVAIKVLRAELGTETLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLV 159
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLAR--HKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKI-YLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 160 MDYID-GEPIDRYCERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEHAEsiap 238
Cdd:cd14003  78 MEYASgGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGS---- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 37520665 239 EASLTVGteqpagvtggalTPEYAAPEQLHG-GAITPITDIYALGVVLYELLHGSRP 294
Cdd:cd14003 154 LLKTFCG------------TPAYAAPEVLLGrKYDGPKADVWSLGVILYAMLTGYLP 198
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
81-294 4.22e-34

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK 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.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 132.21  E-value: 4.22e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  81 YRVVGKLGQGGMGSVYLA-ERADaqySKQVAIKVLRAELGTETLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLV 159
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAvHKKT---GEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNL-YLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 160 MDYID-GEPIDRYCERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVT---AEGMPRLLDFGVAKLLEHAES 235
Cdd:cd05117  78 MELCTgGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAKIFEEGEK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 37520665 236 IapeasltvgtEQPAGvtggalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGSRP 294
Cdd:cd05117 158 L----------KTVCG------TPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPP 200
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
83-290 2.06e-31

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK 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.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 124.71  E-value: 2.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  83 VVGKLGQGGMGSVYLAE-RADAQYskqVAIKVLRAELGTETLVRRFRlERQILADLDHPNIAHLIDGGTTAGGLpYLVMD 161
Cdd:cd13996  10 EIELLGSGGFGSVYKVRnKVDGVT---YAIKKIRLTEKSSASEKVLR-EVKALAKLNHPNIVRYYTAWVEEPPL-YIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 162 YIDGEP----IDRYCERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAE-GMPRLLDFGVAKLLEHAESI 236
Cdd:cd13996  85 LCEGGTlrdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQKRE 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 37520665 237 APEASLTVGTEQPAGvTGGALTPEYAAPEQLHGGAITPITDIYALGVVLYELLH 290
Cdd:cd13996 165 LNNLNNNNNGNTSNN-SVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH 217
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
87-294 5.59e-31

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. 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. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 123.01  E-value: 5.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  87 LGQGGMGSVYLAERADaqySKQV-AIKVLR-AELGTETLVRRFRLERQILADLDHPNIAHLIDGGTTAGGLpYLVMDYID 164
Cdd:cd05123   1 LGKGSFGKVLLVRKKD---TGKLyAMKVLRkKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKL-YLVLDYVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 165 G--------------EPIDRYCerrrlavraRLELFLgvcgAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLL 230
Cdd:cd05123  77 GgelfshlskegrfpEERARFY---------AAEIVL----ALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKEL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37520665 231 EHAESiapeasltvGTEQPAGvtggalTPEYAAPEQLHGGAITPITDIYALGVVLYELLHGSRP 294
Cdd:cd05123 144 SSDGD---------RTYTFCG------TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPP 192
TolBN COG5616
TolB amino-terminal domain (function unknown) [General function prediction only];
399-521 5.69e-31

TolB amino-terminal domain (function unknown) [General function prediction only];


Pssm-ID: 227903  Cd Length: 152  Bit Score: 120.15  E-value: 5.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 399 TVVVLPFSERGSTGD-ERLADGLTLSLTTHLGKVAALTVISDRAAMQYRDSS--LAQIGGDLGATGVLTGSVLRSGERVR 475
Cdd:COG5616  26 SIAVLPFVNLSGDPEqEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAvdVREVGEELGVRYVLEGSVRRAGGRVR 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37520665 476 IAARLVDPRSGTQLWAEQYDRKLQDIFAIQTEVAQRIAAAMKAKLT 521
Cdd:COG5616 106 VTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYG 151
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
87-294 6.62e-30

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 120.35  E-value: 6.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  87 LGQGGMGSVYLAEraDAQYSKQVAIKVL------------RAELGTETLVRRFRLERQILADLDHPNIAHL---IDggtt 151
Cdd:cd14008   1 LGRGSFGKVKLAL--DTETGQLYAIKIFnksrlrkrregkNDRGKIKNALDDVRREIAIMKKLDHPNIVRLyevID---- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 152 aggLP-----YLVMDYIDGEPI---DRYCERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLD 223
Cdd:cd14008  75 ---DPesdklYLVLEYCEGGPVmelDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISD 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37520665 224 FGVAKLLEhaesiaPEASLTVGTeqpAGvtggalTPEYAAPEQLHGGAITPI---TDIYALGVVLYELLHGSRP 294
Cdd:cd14008 152 FGVSEMFE------DGNDTLQKT---AG------TPAFLAPELCDGDSKTYSgkaADIWALGVTLYCLVFGRLP 210
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
87-294 8.53e-30

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or 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. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 119.56  E-value: 8.53e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665  87 LGQGGMGSVYLAE-RadaqySKQVAIKVLRAELGTETLVRRFRLERQILADLDHPNIAHLIdGGTTAGGLPYLVMDYIDG 165
Cdd:cd13999   1 IGSGSFGEVYKGKwR-----GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFI-GACLSPPPLCIVTEYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37520665 166 EPIDRY--CERRRLAVRARLELFLGVCGAVSYAHQRRIVHRDLKPGNILVTAEGMPRLLDFGVAKLLEHaesiapeaslt 243
Cdd:cd13999  75 GSLYDLlhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNS----------- 143
                       170       180       190