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Conserved domains on  [gi|815681805|ref|WP_046417876|]
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serine/threonine-protein kinase [Xylella fastidiosa]

Protein Classification

serine/threonine-protein kinase( domain architecture ID 10013903)

serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12274 PRK12274
serine/threonine protein kinase; Provisional
 2-219 8.50e-145

serine/threonine protein kinase; Provisional


:

Pssm-ID: 237032  Cd Length: 218  Bit Score: 402.36  E-value: 8.50e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805   2 SRPFSVSATLKADCFGRILLVNGKGEKFIRRDLGAVSWWLRGLAGWLARREVAALRQLNTLPAVPRLLNWDGVCLDRSFL 81
Cdd:PRK12274   1 SHPPAVNEPLKSDTFGRILLVRGGERKFVRRDLSAAPWWLRGVAWWLARREALALRQLDGLPRTPRLLHWDGRHLDRSYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  82 SGQMMYQCPPRGDLAYFRAACRLLQQMHRCGVVHNDLAKEANWLVLEDGSPGVIDFQLAVRGDPRAPWMRLLAREDLRHL 161
Cdd:PRK12274  81 AGAAMYQRPPRGDLAYFRAARRLLQQLHRCGVAHNDLAKEANWLVQEDGSPAVIDFQLAVRGNPRARWMRLLAREDLRHL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 815681805 162 LKHKRMYCPEALTPVERRLLKRPSWIRRLWFATGKPVYRFVTRRVLHWEDNEGRGAKP 219
Cdd:PRK12274 161 LKHKRMYCPAALTPVERRVLKRTSWIRELWFATGKPVYRFVTRRVLHWEDNEGQGPKP 218
 
Name Accession Description Interval E-value
PRK12274 PRK12274
serine/threonine protein kinase; Provisional
 2-219 8.50e-145

serine/threonine protein kinase; Provisional


Pssm-ID: 237032  Cd Length: 218  Bit Score: 402.36  E-value: 8.50e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805   2 SRPFSVSATLKADCFGRILLVNGKGEKFIRRDLGAVSWWLRGLAGWLARREVAALRQLNTLPAVPRLLNWDGVCLDRSFL 81
Cdd:PRK12274   1 SHPPAVNEPLKSDTFGRILLVRGGERKFVRRDLSAAPWWLRGVAWWLARREALALRQLDGLPRTPRLLHWDGRHLDRSYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  82 SGQMMYQCPPRGDLAYFRAACRLLQQMHRCGVVHNDLAKEANWLVLEDGSPGVIDFQLAVRGDPRAPWMRLLAREDLRHL 161
Cdd:PRK12274  81 AGAAMYQRPPRGDLAYFRAARRLLQQLHRCGVAHNDLAKEANWLVQEDGSPAVIDFQLAVRGNPRARWMRLLAREDLRHL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 815681805 162 LKHKRMYCPEALTPVERRLLKRPSWIRRLWFATGKPVYRFVTRRVLHWEDNEGRGAKP 219
Cdd:PRK12274 161 LKHKRMYCPAALTPVERRVLKRTSWIRELWFATGKPVYRFVTRRVLHWEDNEGQGPKP 218
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 28-164 5.27e-09

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 53.76  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  28 KFIRRDLGAVSWwlRGLAGWLARREVAALRQL--NTLPaVPRLLNWDGVCLDRSFLSGQMMYQCPPRGDLAYFRAACRLL 105
Cdd:COG0478   27 RRERADKEHYSW--LYAARTRAEREFRALERLypAGLP-VPRPIAANRHAIVMERIEGVELARLKLEDPEEVLDKILEEI 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815681805 106 QQMHRCGVVHNDLAkEANWLVLEDGSPGVIDFQLAVRGDPRApWMRLLAReDLRHLLKH 164
Cdd:COG0478  104 RRAHDAGIVHADLS-EYNILVDDDGGVWIIDWPQAVPRDHPN-AEELLER-DLENLLRS 159
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 47-164 6.84e-07

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695 [Multi-domain]  Cd Length: 183  Bit Score: 47.88  E-value: 6.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  47 WL------ARREVAALRQL--NTLPaVPRLLNWDGVCLDRSFLSGQMMYQCPPRGDLA-YFRAACRLLQQMHRCGVVHND 117
Cdd:cd05144   57 WLylsrlaAEKEFAALKALyeEGFP-VPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEeVLDEILELIVKLAKHGLIHGD 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 815681805 118 LAkEANWLVLEDGSPGVIDFQLAV-RGDPRAPWmrLLAReDLRHLLKH 164
Cdd:cd05144  136 FS-EFNILVDEDEKITVIDFPQMVsTSHPNAEE--YFDR-DVECIIKF 179
 
Name Accession Description Interval E-value
PRK12274 PRK12274
serine/threonine protein kinase; Provisional
 2-219 8.50e-145

serine/threonine protein kinase; Provisional


Pssm-ID: 237032  Cd Length: 218  Bit Score: 402.36  E-value: 8.50e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805   2 SRPFSVSATLKADCFGRILLVNGKGEKFIRRDLGAVSWWLRGLAGWLARREVAALRQLNTLPAVPRLLNWDGVCLDRSFL 81
Cdd:PRK12274   1 SHPPAVNEPLKSDTFGRILLVRGGERKFVRRDLSAAPWWLRGVAWWLARREALALRQLDGLPRTPRLLHWDGRHLDRSYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  82 SGQMMYQCPPRGDLAYFRAACRLLQQMHRCGVVHNDLAKEANWLVLEDGSPGVIDFQLAVRGDPRAPWMRLLAREDLRHL 161
Cdd:PRK12274  81 AGAAMYQRPPRGDLAYFRAARRLLQQLHRCGVAHNDLAKEANWLVQEDGSPAVIDFQLAVRGNPRARWMRLLAREDLRHL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 815681805 162 LKHKRMYCPEALTPVERRLLKRPSWIRRLWFATGKPVYRFVTRRVLHWEDNEGRGAKP 219
Cdd:PRK12274 161 LKHKRMYCPAALTPVERRVLKRTSWIRELWFATGKPVYRFVTRRVLHWEDNEGQGPKP 218
PRK09188 PRK09188
serine/threonine protein kinase; Provisional
 5-216 8.15e-67

serine/threonine protein kinase; Provisional


Pssm-ID: 236400 [Multi-domain]  Cd Length: 365  Bit Score: 209.62  E-value: 8.15e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805   5 FSVSATLKADCF-----GRILLVNGKGEKfIRRDLGAVSWWLRGLAGWLARREVAALRQLNTLPAVPRLLNWDGVCLDRS 79
Cdd:PRK09188  20 FVETAVLKRDVFstverGYFAGDPGTARA-VRRRVSEVPWWSKPLARHLAAREIRALKTVRGIGVVPQLLATGKDGLVRG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  80 FLSGQMMYQCPPRGDLAYFRAACRLLQQMHRCGVVHNDLAKEANWLVLEDGSPGVIDFQLAVRGDPRAPWMRLLAREDLR 159
Cdd:PRK09188  99 WTEGVPLHLARPHGDPAWFRSAHRALRDLHRAGITHNDLAKPQNWLMGPDGEAAVIDFQLASVFRRRGALYRIAAYEDLR 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815681805 160 HLLKHKRMYCPEALTPVERRLLKRPSWIRRLWFATGKPVYRFVTRRVLHWEDNEGRG 216
Cdd:PRK09188 179 HLLKHKRTYAPDALTPRERKILARKSLPSRIWLATGKKVYNFITRGLFSWSDGEGTG 235
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 28-164 5.27e-09

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 53.76  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  28 KFIRRDLGAVSWwlRGLAGWLARREVAALRQL--NTLPaVPRLLNWDGVCLDRSFLSGQMMYQCPPRGDLAYFRAACRLL 105
Cdd:COG0478   27 RRERADKEHYSW--LYAARTRAEREFRALERLypAGLP-VPRPIAANRHAIVMERIEGVELARLKLEDPEEVLDKILEEI 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815681805 106 QQMHRCGVVHNDLAkEANWLVLEDGSPGVIDFQLAVRGDPRApWMRLLAReDLRHLLKH 164
Cdd:COG0478  104 RRAHDAGIVHADLS-EYNILVDDDGGVWIIDWPQAVPRDHPN-AEELLER-DLENLLRS 159
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 49-145 8.68e-08

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 49.96  E-value: 8.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  49 ARREVAALRQLNT--LPaVPRLL--NWDGVCLDRSFLSGQMMYQCPPRGDL--AYFRAACRLLQQMHRCGVVHNDLAkeA 122
Cdd:COG3642    3 TRREARLLRELREagVP-VPKVLdvDPDDADLVMEYIEGETLADLLEEGELppELLRELGRLLARLHRAGIVHGDLT--T 79

                         90       100
                 ....*....|....*....|...
gi 815681805 123 NWLVLEDGSPGVIDFQLAVRGDP 145
Cdd:COG3642   80 SNILVDDGGVYLIDFGLARYSDP 102
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
49-166 2.84e-07

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 49.25  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  49 ARREVAALRQLNTLPAVPRLLNWDGVCLDRSFLSGQMMYQCPPRGD----LAYFRAACRLLQQMHRCGVVHNDLAKEANW 124
Cdd:COG2112   80 LKKEAEILKKANGAGVGPKLYDYGRDFLVMEYIEGEPLKDWLENLDkeelRKVIRELLEAAYLLDRIGIDHGELSRPGKH 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815681805 125 LVLEDGSPGVIDFQLA----------------VRGDPRAPWMR---LLAREDLRHLLKHKR 166
Cdd:COG2112  160 VIVDKGRPYIIDFESAsisrkpsnvtsalsylFLGSNIAKRIKkilGLDKEKLRELLKLYK 220
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 47-164 6.84e-07

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695 [Multi-domain]  Cd Length: 183  Bit Score: 47.88  E-value: 6.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  47 WL------ARREVAALRQL--NTLPaVPRLLNWDGVCLDRSFLSGQMMYQCPPRGDLA-YFRAACRLLQQMHRCGVVHND 117
Cdd:cd05144   57 WLylsrlaAEKEFAALKALyeEGFP-VPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEeVLDEILELIVKLAKHGLIHGD 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 815681805 118 LAkEANWLVLEDGSPGVIDFQLAV-RGDPRAPWmrLLAReDLRHLLKH 164
Cdd:cd05144  136 FS-EFNILVDEDEKITVIDFPQMVsTSHPNAEE--YFDR-DVECIIKF 179
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 95-140 7.50e-05

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: 42.57  E-value: 7.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 815681805  95 LAYFRAACRLLQQMHRCGVVHNDLaKEANWLVLEDGSPGVIDFQLA 140
Cdd:cd14014  103 LRILAQIADALAAAHRAGIVHRDI-KPANILLTEDGRVKLTDFGIA 147
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
50-140 1.26e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 42.31  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815681805  50 RREVAALRQLNtLPAVPRLLNW--------------DGVCLDRSFLSGQMMyqcPPRGDLAYFRAACRLLQQMHRCGVVH 115
Cdd:COG0515   55 RREARALARLN-HPNIVRVYDVgeedgrpylvmeyvEGESLADLLRRRGPL---PPAEALRILAQLAEALAAAHAAGIVH 130

                         90       100
                 ....*....|....*....|....*
gi 815681805 116 NDLaKEANWLVLEDGSPGVIDFQLA 140
Cdd:COG0515  131 RDI-KPANILLTPDGRVKLIDFGIA 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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