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Conserved domains on  [gi|15807503|ref|NP_296238|]
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DNA damage-responsive serine/threonine-protein kinase RqkA [Deinococcus radiodurans R1]

Protein Classification

Graphical summary

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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 ...
12-264 5.51e-94

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  Cd Length: 260  Bit Score: 294.49  E-value: 5.51e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  12 RYELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESD--RSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFT 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEefRERFLREARALARLSHPNIVRVYDVGEDD--GRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  90 MPLLTGGP----ITRLGPLedapgPLARFLTAAAFASRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLvALSEQT 165
Cdd:cd14014  79 MEYVEGGSladlLRERGPL-----PPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGI-ARALGD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 166 RHLTRSGVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNPAVPDAV 245
Cdd:cd14014 153 SGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250
                ....*....|....*....
gi 15807503 246 ARVLLWLLAKRADRRPQSG 264
Cdd:cd14014 233 DAIILRALAKDPEERPQSA 251
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
310-660 9.61e-34

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 224437  Cd Length: 370  Bit Score: 133.47  E-value: 9.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 310 LWSVAlPGEVTWPAAVVGEGDLVAVGTRGGQLVLTHTSGRPFATYAardevTAPATLIGGHVLYGAWDGTLRRVELQSGS 389
Cdd:COG1520  16 ATPVL-AAGTDYLVAVGADLVAVANNTSGTLLWSVSLGSGGGGIYA-----GPAPADGDGTVYVGTRDGNIFALNPDTGL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 390 EVWRH---QARAEFTGAPTVWGGRLLAPSRDGHLHALSLRTGELAWAYRAGGS--LAASPLVWAGAALQCDETGWLHALD 464
Cdd:COG1520  90 VKWSYpllGAVAQLSGPILGSDGKIYVGSWDGKLYALDASTGTLVWSRNVGGSpyYASPPVVGDGTVYVGTDDGHLYALN 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 465 ARSGTPLWKVEVGTvhATPALLPGPPGTA--TLVIATWEGEVHAIGLEVQNGraalagedAIRWTYDVEDEVWAspalTA 542
Cdd:COG1520 170 ADTGTLKWTYETPA--PLSLSIYGSPAIAsgTVYVGSDGYDGILYALNAEDG--------TLKWSQKVSQTIGR----TA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 543 LDLPPDSGAAPDASAAPGGVVVVAGWGGkvrGLRLADGEDLWERTLDGRVTASPVISA------GLVFLATEGGE----- 611
Cdd:COG1520 236 ISTTPAVDGGPVYVDGGVYAGSYGGKLL---CLDADTGELIWSFPAGGSVQGSGLYTTpvagadGKVYIGFTDNDgrgsg 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15807503 612 -LLALDVRNG--EVRWTCRERSGVQATPLAAS-GTLYVAFMDG-TLRAYRNAHP 660
Cdd:COG1520 313 sLYALADVPGgtLLKWSYPVGGGYSLSTVAGSdGTLYFGGDDGrGLYAFRDGAL 366
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
12-264 5.51e-94

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  Cd Length: 260  Bit Score: 294.49  E-value: 5.51e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  12 RYELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESD--RSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFT 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEefRERFLREARALARLSHPNIVRVYDVGEDD--GRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  90 MPLLTGGP----ITRLGPLedapgPLARFLTAAAFASRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLvALSEQT 165
Cdd:cd14014  79 MEYVEGGSladlLRERGPL-----PPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGI-ARALGD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 166 RHLTRSGVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNPAVPDAV 245
Cdd:cd14014 153 SGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250
                ....*....|....*....
gi 15807503 246 ARVLLWLLAKRADRRPQSG 264
Cdd:cd14014 233 DAIILRALAKDPEERPQSA 251
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-261 1.22e-57

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 197.75  E-value: 1.22e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503     13 YELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFTMPL 92
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503     93 LTGGP----ITRLGPLEDapgPLARFLTAAAFasRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLVALSEQTRHL 168
Cdd:smart00220  79 CEGGDlfdlLKKRGRLSE---DEARFYLRQIL--SALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    169 TrsgVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNPAVPDAVARV 248
Cdd:smart00220 154 T---TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|...
gi 15807503    249 LLWLLAKRADRRP 261
Cdd:smart00220 231 IRKLLVKDPEKRL 243
Pkinase pfam00069
Protein kinase domain;
13-261 1.36e-41

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 152.37  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    13 YELLALLGEGGSAQVYRAQDGLLGREVALKVM-HDYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFTMP 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDK--DNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    92 LLTGGPITRL----GPLEDApgpLARFLTAAAFasRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLVALSEQTRH 167
Cdd:pfam00069  79 YVEGGSLFDLlsekGAFSER---EAKFIMKQIL--EGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   168 LTrSGVtlGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDlnPAVPDAVAR 247
Cdd:pfam00069 154 LT-SFV--GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRP--SSISEEAKD 228
                         250
                  ....*....|....
gi 15807503   248 VLLWLLAKRADRRP 261
Cdd:pfam00069 229 LLKKLLKKDPSKRL 242
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-263 7.82e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 148.35  E-value: 7.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  13 YELLALLGEGGSAQVYRAQDGllgREVALKVMH--DYLPESDRSRFLREVRTLARLTHPG-VVPVLDLGQEPeaGRPFFT 89
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAkkLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQDE--GSLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  90 MPLLTGGPITRLGPLEDAPGPLARFLTAAAFAS--RALHHVHSHGIVHRDLTPGNVLLD-DTGLPRIMDFGLVALSEQTR 166
Cdd:COG0515  77 MEYVDGGSLEDLLKKIGRKGPLSESEALFILAQilSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAKLLPDPG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 167 ----HLTRSGVTLGTPAYMAPEQAKG---GGVDARSDLYALGAVLYRVACGSPPF---VGDSDQSVLYQHVYE------P 230
Cdd:COG0515 157 stssIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILElptpslA 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 15807503 231 VPDPRDLNPAVPDAVARVLLWLLAKRADRRPQS 263
Cdd:COG0515 237 SPLSPSNPELISKAASDLLKKLLAKDPKNRLSS 269
pknD PRK13184
serine/threonine-protein kinase; Reviewed
11-263 4.12e-36

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 145.30  E-value: 4.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   11 GRYELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESD--RSRFLREVRTLARLTHPGVVPVLDLGQEPEAgrPFF 88
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPllKKRFLREAKIAADLIHPGIVPVYSICSDGDP--VYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   89 TMPLLTGGPITRL----GPLEDAPGPLARFLTAAAFAS------RALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGL 158
Cdd:PRK13184  80 TMPYIEGYTLKSLlksvWQKESLSKELAEKTSVGAFLSifhkicATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  159 VALSEQTR----------------HLTRSGVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSV 222
Cdd:PRK13184 160 AIFKKLEEedlldidvdernicysSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15807503  223 LYQHVyepVPDPRDLNP--AVPDAVARVLLWLLAKRADRRPQS 263
Cdd:PRK13184 240 SYRDV---ILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSS 279
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
310-660 9.61e-34

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224437  Cd Length: 370  Bit Score: 133.47  E-value: 9.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 310 LWSVAlPGEVTWPAAVVGEGDLVAVGTRGGQLVLTHTSGRPFATYAardevTAPATLIGGHVLYGAWDGTLRRVELQSGS 389
Cdd:COG1520  16 ATPVL-AAGTDYLVAVGADLVAVANNTSGTLLWSVSLGSGGGGIYA-----GPAPADGDGTVYVGTRDGNIFALNPDTGL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 390 EVWRH---QARAEFTGAPTVWGGRLLAPSRDGHLHALSLRTGELAWAYRAGGS--LAASPLVWAGAALQCDETGWLHALD 464
Cdd:COG1520  90 VKWSYpllGAVAQLSGPILGSDGKIYVGSWDGKLYALDASTGTLVWSRNVGGSpyYASPPVVGDGTVYVGTDDGHLYALN 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 465 ARSGTPLWKVEVGTvhATPALLPGPPGTA--TLVIATWEGEVHAIGLEVQNGraalagedAIRWTYDVEDEVWAspalTA 542
Cdd:COG1520 170 ADTGTLKWTYETPA--PLSLSIYGSPAIAsgTVYVGSDGYDGILYALNAEDG--------TLKWSQKVSQTIGR----TA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 543 LDLPPDSGAAPDASAAPGGVVVVAGWGGkvrGLRLADGEDLWERTLDGRVTASPVISA------GLVFLATEGGE----- 611
Cdd:COG1520 236 ISTTPAVDGGPVYVDGGVYAGSYGGKLL---CLDADTGELIWSFPAGGSVQGSGLYTTpvagadGKVYIGFTDNDgrgsg 312
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15807503 612 -LLALDVRNG--EVRWTCRERSGVQATPLAAS-GTLYVAFMDG-TLRAYRNAHP 660
Cdd:COG1520 313 sLYALADVPGgtLLKWSYPVGGGYSLSTVAGSdGTLYFGGDDGrGLYAFRDGAL 366
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
36-263 1.10e-23

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  Cd Length: 1266  Bit Score: 106.85  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503     36 GREVALKVMHDYLPESDR--SRFLREVRTLARLTHPGVVPVLDLGQEPEaGRPFFTMPLLTGgpiTRLGPLEDAPGPLAR 113
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHqrARFRRETALCARLYHPNIVALLDSGEAPP-GLLFAVFEYVPG---RTLREVLAADGALPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    114 FLTAAAFAS--RALHHVHSHGIVHRDLTPGNVLLDDTGLPR---IMDFGLVALSEQTR-----HLTRSGVTLGTPAYMAP 183
Cdd:TIGR03903   79 GETGRLMLQvlDALACAHNQGIVHRDLKPQNIMVSQTGVRPhakVLDFGIGTLLPGVRdadvaTLTRTTEVLGTPTYCAP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    184 EQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVyepVPDPRDLNPAVPD-AVARVLLWLLAKRADRRPQ 262
Cdd:TIGR03903  159 EQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQL---SPVDVSLPPWIAGhPLGQVLRKALNKDPRQRAA 235

                   .
gi 15807503    263 S 263
Cdd:TIGR03903  236 S 236
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
377-625 3.02e-19

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


Pssm-ID: 315925  Cd Length: 233  Bit Score: 88.23  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   377 DGTLRRVELQSGSEVWRHQARAEFTGAPTVWGGRLLAPSRDGHLHALSLRTGELAWAYRAGGSLAASPLVWAGAALQCDE 456
Cdd:pfam13360   2 DGTVSALDAATGAELWRVDLGTPLGGGVAVDGGTLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGGRVFVVAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   457 TGWLHALDARSGTPLWKVEvGTVHATPALLPGPP--GTATLVIATWEGEVHAigLEVQNGRAalagedaiRWtydvEDEV 534
Cdd:pfam13360  82 DGSLAALDAETGKRLWSYQ-RSGPPLALRSSGSPavAGDTVVVGFASGKLVA--LDPKTGKV--------RW----EAPL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   535 WASPALTALDLPPDSGAAP-------DASAAPGGVVVvagwggkvrgLRLADGEDLWERTLDGRVtaSPVISAGLVFLAT 607
Cdd:pfam13360 147 AAPRGTNELERLVDITGTPvvdggrvCAVSYQGRLGA----------FDAATGRVLWSRDISSIN--GPAVDGDLLYVVD 214
                         250
                  ....*....|....*...
gi 15807503   608 EGGELLALDVRNGEVRWT 625
Cdd:pfam13360 215 DDGEVYALDRATGAVLWK 232
BamB_YfgL cd10276
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ...
402-655 2.38e-17

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  Cd Length: 358  Bit Score: 83.92  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 402 GAPTVWGGRLLAPSRDGHLHALSLRTGELAWAYRAGGS--LAASPLVWAGAALQCDETGWLHALDARSGTPLWKVEVgtv 479
Cdd:cd10276  32 LTPVVAGDMVYAADANGQVSAFNATTGKIIWETSLSGKgfLGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEV--- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 480 haTPALLPGPPGTA--TLVIATWEGEVHAIglevqngraaLAGEDAIRWTYDVedevwASPALTAldlppDSGAAPdasA 557
Cdd:cd10276 109 --SDSQLLSPPTYAdgKIYVGTGDGRLYYC----------NAETGKVVWNRTS-----TAPELSL-----RGGAAP---V 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 558 APGGVVVVAGWGGKVRGLRLADGEDLWE---------RTLDG--RVTASPVISAGLVFLATEGGELLALDVRNGEVRWTc 626
Cdd:cd10276 164 GAYDVVFVGDGNGTVVALNTGTGVDIWEfsvseprgrTELPRmiDSSVTYVVVGGYLYSTSYQGYLVALDFESGQFLWS- 242
                       250       260
                ....*....|....*....|....*....
gi 15807503 627 RERSGVQATPLAASGTLYVAFMDGTLRAY 655
Cdd:cd10276 243 RKASGGTSTSTDANGRVYVGDGEGSLYCL 271
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
306-656 7.54e-16

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: 274511  Cd Length: 377  Bit Score: 79.59  E-value: 7.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   306 DMQELWSVAL---PGEVTWPAAVVGEGDLVAVGTRGGQLV-LTHTSGRPFATYAARDEVTAPATLIGGHVLYGAWDGTLR 381
Cdd:TIGR03300  39 KVDQVWSASVgdgVGHYYLRLQPAVAGGKVYAADADGTVAaLDAETGKRLWRVDLDERLSGGVGADGGLVFVGTEKGEVI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   382 RVELQSGSEVWRHQARAEFTGAPTVWGGRLLAPSRDGHLHALSLRTGELAWAYR----------AGGSLAASPLVWAGAA 451
Cdd:TIGR03300 119 ALDAEDGKELWRAKLSSEVLSPPLVANGLVVVRTNDGRLTALDAATGERLWTYSrvtppltlrgSASPVIADGGVLVGFA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   452 LqcdetGWLHALDARSGTPLWKVEVGT------------VHATPALLPGppgtaTLVIATWEGEVHAigLEVQNGRaala 519
Cdd:TIGR03300 199 G-----GKLVALDLQTGQPLWEQRVALpkgrtelerlvdVDGDPVVDGG-----QVYAVSYQGRVAA--LDLRSGR---- 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   520 gedairwtydvedEVWASPALTALDLPPDSGA--APDASAApggvvvvagwggkVRGLRLADGEDLWERT-LDGRVTASP 596
Cdd:TIGR03300 263 -------------VLWKRDASSYQGPAVDDNRlyVTDADGV-------------VVALDRRSGSELWKNDeLKYRQLTAP 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   597 VISAGLV----------FLATEGGELLALDVRNGevrwtcrerSGVQATPLAASGTLYVAFMDGTLRAYR 656
Cdd:TIGR03300 317 AVLGGYLvvgdfegylhWLDRDDGSFVARLKTDG---------SGIASPPVVVGDGLLVQTRDGDLYAFR 377
PRK11138 PRK11138
outer membrane biogenesis protein BamB; Provisional
404-645 1.34e-09

outer membrane biogenesis protein BamB; Provisional


Pssm-ID: 236857  Cd Length: 394  Bit Score: 60.33  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  404 PTVWGGRLLAPSRDGHLHALSLRTGELAW----------------AYRAGGSLAASPLVWAGAalqcdETGWLHALDARS 467
Cdd:PRK11138  65 PAVAYNKVYAADRAGLVKALDADTGKEIWsvdlsekdgwfsknksALLSGGVTVAGGKVYIGS-----EKGQVYALNAED 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  468 GTPLWKVEV-GTVHATPALlpgppGTATLVIATWEGEVhaIGLEVQNGraalagedAIRWTYDVEdevwaSPALTaldLP 546
Cdd:PRK11138 140 GEVAWQTKVaGEALSRPVV-----SDGLVLVHTSNGML--QALNESDG--------AVKWTVNLD-----VPSLT---LR 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  547 PDSGAAPDASAApggvvvvagWGGKVRGlRLA-----DGEDLWE-------------RTLDgrVTASPVISAGLVFLATE 608
Cdd:PRK11138 197 GESAPATAFGGA---------IVGGDNG-RVSavlmeQGQLIWQqrisqptgateidRLVD--VDTTPVVVGGVVYALAY 264
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15807503  609 GGELLALDVRNGEVRWTcRERSGVqaTPLAASG-TLYV 645
Cdd:PRK11138 265 NGNLVALDLRSGQIVWK-REYGSV--NDFAVDGgRIYL 299
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
12-264 5.51e-94

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  Cd Length: 260  Bit Score: 294.49  E-value: 5.51e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  12 RYELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESD--RSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFT 89
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEefRERFLREARALARLSHPNIVRVYDVGEDD--GRPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  90 MPLLTGGP----ITRLGPLedapgPLARFLTAAAFASRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLvALSEQT 165
Cdd:cd14014  79 MEYVEGGSladlLRERGPL-----PPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGI-ARALGD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 166 RHLTRSGVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNPAVPDAV 245
Cdd:cd14014 153 SGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250
                ....*....|....*....
gi 15807503 246 ARVLLWLLAKRADRRPQSG 264
Cdd:cd14014 233 DAIILRALAKDPEERPQSA 251
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-261 1.22e-57

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 197.75  E-value: 1.22e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503     13 YELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFTMPL 92
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDE--DKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503     93 LTGGP----ITRLGPLEDapgPLARFLTAAAFasRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLVALSEQTRHL 168
Cdd:smart00220  79 CEGGDlfdlLKKRGRLSE---DEARFYLRQIL--SALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    169 TrsgVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNPAVPDAVARV 248
Cdd:smart00220 154 T---TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDL 230
                          250
                   ....*....|...
gi 15807503    249 LLWLLAKRADRRP 261
Cdd:smart00220 231 IRKLLVKDPEKRL 243
Pkinase pfam00069
Protein kinase domain;
13-261 1.36e-41

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 152.37  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    13 YELLALLGEGGSAQVYRAQDGLLGREVALKVM-HDYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFTMP 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDK--DNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503    92 LLTGGPITRL----GPLEDApgpLARFLTAAAFasRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLVALSEQTRH 167
Cdd:pfam00069  79 YVEGGSLFDLlsekGAFSER---EAKFIMKQIL--EGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFGLARQLNSGSS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   168 LTrSGVtlGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDlnPAVPDAVAR 247
Cdd:pfam00069 154 LT-SFV--GTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDFDSPRP--SSISEEAKD 228
                         250
                  ....*....|....
gi 15807503   248 VLLWLLAKRADRRP 261
Cdd:pfam00069 229 LLKKLLKKDPSKRL 242
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
19-205 1.38e-41

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  Cd Length: 215  Bit Score: 151.27  E-value: 1.38e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  19 LGEGGSAQVYRAQDGLLGREVALKVMHDYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFTMPLLTGGPI 98
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETE--NFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  99 TRLGPLEDAPGPLARFLTAAAFASRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGLVALSEQTRHLTRSGVTLGTP 178
Cdd:cd00180  79 KDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPP 158
                       170       180
                ....*....|....*....|....*..
gi 15807503 179 AYMAPEQAKGGGVDARSDLYALGAVLY 205
Cdd:cd00180 159 YYAPPELLGGRYYGPKVDIWSLGVILY 185
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-263 7.82e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 148.35  E-value: 7.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  13 YELLALLGEGGSAQVYRAQDGllgREVALKVMH--DYLPESDRSRFLREVRTLARLTHPG-VVPVLDLGQEPeaGRPFFT 89
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAkkLESKSKEVERFLREIQILASLNHPPnIVKLYDFFQDE--GSLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  90 MPLLTGGPITRLGPLEDAPGPLARFLTAAAFAS--RALHHVHSHGIVHRDLTPGNVLLD-DTGLPRIMDFGLVALSEQTR 166
Cdd:COG0515  77 MEYVDGGSLEDLLKKIGRKGPLSESEALFILAQilSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAKLLPDPG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 167 ----HLTRSGVTLGTPAYMAPEQAKG---GGVDARSDLYALGAVLYRVACGSPPF---VGDSDQSVLYQHVYE------P 230
Cdd:COG0515 157 stssIPALPSTSVGTPGYMAPEVLLGlslAYASSSSDIWSLGITLYELLTGLPPFegeKNSSATSQTLKIILElptpslA 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 15807503 231 VPDPRDLNPAVPDAVARVLLWLLAKRADRRPQS 263
Cdd:COG0515 237 SPLSPSNPELISKAASDLLKKLLAKDPKNRLSS 269
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-261 9.64e-37

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  Cd Length: 252  Bit Score: 138.80  E-value: 9.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  12 RYELLALLGEGGSAQVYRAQDGLLGREVALKVMH-DYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPeaGRPFFTM 90
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDkSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETE--NKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  91 PLLTGGP----ITRLGPL-EDapgpLARFLtaaaFA--SRALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGlvaLSE 163
Cdd:cd14003  79 EYASGGElfdyIVNNGRLsED----EARRF----FQqlISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG---LSN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503 164 QTRHLTRSGVTLGTPAYMAPEQAKGGGVDAR-SDLYALGAVLYRVACGSPPFVGDSDQSVLYQHVYEPVPDPRDLNpavP 242
Cdd:cd14003 148 EFRGGSLLKTFCGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLS---P 224
                       250
                ....*....|....*....
gi 15807503 243 DAVaRVLLWLLAKRADRRP 261
Cdd:cd14003 225 DAR-DLIRRMLVVDPSKRI 242
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-225 1.12e-36

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  Cd Length: 258  Bit Score: 138.76  E-value: 1.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  12 RYELLALLGEGGSAQVYRAQDGLLGREVALKVMH-DYLPESDRSRFLREVRTLARLTHPGVVPVLDLGQEPEagRPFFTM 90
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDkKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDK--NLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  91 PLLTGGP----ITRLGPLEDApgpLARFLTAAAFasRALHHVHSHGIVHRDLTPGNVLLDDT---GLPRIMDFGLVALSE 163
Cdd:cd05117  79 ELCTGGElfdrIVKKGSFSER---EAAKIMKQIL--SAVAYLHSQGIVHRDLKPENILLASKdpdSPIKIIDFGLAKIFE 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15807503 164 QTRHLTrsgVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSVLYQ 225
Cdd:cd05117 154 EGEKLK---TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEK 212
pknD PRK13184
serine/threonine-protein kinase; Reviewed
11-263 4.12e-36

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 145.30  E-value: 4.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   11 GRYELLALLGEGGSAQVYRAQDGLLGREVALKVMHDYLPESD--RSRFLREVRTLARLTHPGVVPVLDLGQEPEAgrPFF 88
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPllKKRFLREAKIAADLIHPGIVPVYSICSDGDP--VYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503   89 TMPLLTGGPITRL----GPLEDAPGPLARFLTAAAFAS------RALHHVHSHGIVHRDLTPGNVLLDDTGLPRIMDFGL 158
Cdd:PRK13184  80 TMPYIEGYTLKSLlksvWQKESLSKELAEKTSVGAFLSifhkicATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15807503  159 VALSEQTR----------------HLTRSGVTLGTPAYMAPEQAKGGGVDARSDLYALGAVLYRVACGSPPFVGDSDQSV 222
Cdd:PRK13184 160 AIFKKLEEedlldidvdernicysSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15807503  223 LYQHVyepVPDPRDLNP--AVPDAVARVLLWLLAKRADRRPQS 263
Cdd:PRK13184 240 SYRDV---ILSPIEVAPyrEIPPFLSQIAMKALAVDPAERYSS 279
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-249 4.58e-35

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase,