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Conserved domains on  [gi|145339355|ref|NP_190695|]
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protein serine/threonine kinase [Arabidopsis thaliana]

Protein Classification

serine/threonine-protein kinase RIO2( domain architecture ID 10557840)

serine/threonine-protein kinase RIO2 is an atypical serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Symbol:  RIOK2
Gene Ontology:  GO:0005524|GO:0004674|GO:0006468
PubMed:  16183636|16182620|19614568|16244704

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 93-274 5.39e-120

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: 347.95  E-value: 5.39e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  93 TGVGRQIGVGKESDIFEVAQEDGTILAMKLHRLGRTSFRAVKSKRDYLRHRSSFSWLYLSRLAALKEFAFMKALEEHDFP 172
Cdd:cd05144    2 SSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFAALKALYEEGFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 173 VPKAIDCNRHCVIMSLVQGYPMVQVKQLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDFPQMVSVS 252
Cdd:cd05144   82 VPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEKITVIDFPQMVSTS 161

                        170       180
                 ....*....|....*....|..
gi 145339355 253 HRNAQMYFDRDIECIFKFFRKR 274
Cdd:cd05144  162 HPNAEEYFDRDVECIIKFFRRK 183
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 8-89 2.32e-33

Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to the winged helix (wHTH) domain. They adopt a structure consisting of four alpha helices followed by two beta strands and a fifth alpha helix. The domain confers DNA binding properties to the protein, as per other winged helix domains.


:

Pssm-ID: 462715  Cd Length: 82  Bit Score: 120.73  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355    8 LRYLSKDDFRVLTAVEMGMRNHEIVPSELVERIACLKHGGTYKVLKNLLKYKLLHHDSSKYDGFRLTYLGYDFLAIKTLV 87
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRHGGVNKRLSRLAKRKLISRKNAKYDGYRLTYLGYDYLALRTLV 80


                  ..
gi 145339355   88 NR 89
Cdd:pfam09202  81 KR 82
 
Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 93-274 5.39e-120

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: 347.95  E-value: 5.39e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  93 TGVGRQIGVGKESDIFEVAQEDGTILAMKLHRLGRTSFRAVKSKRDYLRHRSSFSWLYLSRLAALKEFAFMKALEEHDFP 172
Cdd:cd05144    2 SSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFAALKALYEEGFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 173 VPKAIDCNRHCVIMSLVQGYPMVQVKQLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDFPQMVSVS 252
Cdd:cd05144   82 VPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEKITVIDFPQMVSTS 161

                        170       180
                 ....*....|....*....|..
gi 145339355 253 HRNAQMYFDRDIECIFKFFRKR 274
Cdd:cd05144  162 HPNAEEYFDRDVECIIKFFRRK 183
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 106-283 1.15e-72

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


Pssm-ID: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 227.12  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  106 DIFEVAQEDGTILAMKLHRLGRTSFRAVKSKRDYLRHR--SSFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCNRHC 183
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFrdRKTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  184 VIMSLV--QGYPMVQVKQLQ--NPETIFEKIIGIVVRL-AEHGLIHCDFNEFNIMIDDeEKITMIDFPQMVSVSHRNAQM 258
Cdd:pfam01163  81 LVMEFIgkDGVPAPKLKDVEleEAEEIYDEIIREMRRLyQEAGLVHGDLSEYNILVHD-DKPVIIDVPQAVETDHPNALE 159

                         170       180
                  ....*....|....*....|....*
gi 145339355  259 YFDRDIECIFKFFRKRFNMSFHEDK 283
Cdd:pfam01163 160 FLERDVENIINFFRRKGVDEVDERK 184
RIO smart00090
RIO-like kinase;
64-274 3.23e-55

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 183.66  E-value: 3.23e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355    64 DSSKYDGFRLTYLGYDFLAIKTLVNRGIFTGVGRQIGVGKESDIFEV--AQEDGTILAMKLHRLGRTSFRAVKSKRDYLR 141
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAldFDGSGKERAVKIYRTGTLEFKRRDRYVDGDF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355   142 --HRSSFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCNRHCVIMSLV--QGYPMVQVKQLQN----PETIFEKIIGI 213
Cdd:smart00090  81 rfKYRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIggDGLPAPRLKDVEPeeeeEFELYDDILEE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145339355   214 VVRLAEHG-LIHCDFNEFNIMIDDeEKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFFRKR 274
Cdd:smart00090 161 MRKLYKEGeLVHGDLSEYNILVHD-GKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRK 221
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 112-277 2.50e-52

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: 174.32  E-value: 2.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 112 QEDGTILAMKLHRLGRTSFRAVKSKRDYLRHrssFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCNRHCVIMSLVQG 191
Cdd:COG0478    5 SPGGGPVALKFHREGRTSFRKVRRERADKEH---YSWLYAARTRAEREFRALERLYPAGLPVPRPIAANRHAIVMERIEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 192 YPMVQVKqLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFF 271
Cdd:COG0478   82 VELARLK-LEDPEEVLDKILEEIRRAHDAGIVHADLSEYNILVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSF 160


                 ....*.
gi 145339355 272 RKRFNM 277
Cdd:COG0478  161 RKKYGL 166
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 8-89 2.32e-33

Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to the winged helix (wHTH) domain. They adopt a structure consisting of four alpha helices followed by two beta strands and a fifth alpha helix. The domain confers DNA binding properties to the protein, as per other winged helix domains.


Pssm-ID: 462715  Cd Length: 82  Bit Score: 120.73  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355    8 LRYLSKDDFRVLTAVEMGMRNHEIVPSELVERIACLKHGGTYKVLKNLLKYKLLHHDSSKYDGFRLTYLGYDFLAIKTLV 87
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRHGGVNKRLSRLAKRKLISRKNAKYDGYRLTYLGYDYLALRTLV 80


                  ..
gi 145339355   88 NR 89
Cdd:pfam09202  81 KR 82
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 140-245 6.36e-10

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 59.13  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 140 LRH-----------RSSFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCN--RHCV------IMSLVQGypmVQ--VK 198
Cdd:PRK01723  60 LRHyrrggligklsKDRYLFTGLERTRAFAEFRLLAQLYEAGLPVPRPIAARvvRHGLfyradiLIERIEG---ARdlVA 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145339355 199 QLQN---PETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDF 245
Cdd:PRK01723 137 LLQEaplSEEQWQAIGQLIARFHDAGVYHADLNAHNILLDPDGKFWLIDF 186
lanthi_synth_III NF038151
class III lanthionine synthetase LanKC;
153-245 4.23e-05

class III lanthionine synthetase LanKC;


Pssm-ID: 468387 [Multi-domain]  Cd Length: 831  Bit Score: 46.01  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 153 RLAalKEFAFMKALEEHDFpVPKAIDCNR----HCVIMSLVQGYPMVQVKQLQNP------------------ETIFEKI 210
Cdd:NF038151 269 RLR--REREALERLAGLGG-VPEVIDYFTvwehHFLVEEFVEGRPLNSWLARRYPltradpdpealaaytewaLRILRQV 345

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145339355 211 IGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDF 245
Cdd:NF038151 346 ERAVAAVHARGVVFGDLHPFNIMVDPDGSVRLIDF 380
 
Name Accession Description Interval E-value
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 93-274 5.39e-120

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: 347.95  E-value: 5.39e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  93 TGVGRQIGVGKESDIFEVAQEDGTILAMKLHRLGRTSFRAVKSKRDYLRHRSSFSWLYLSRLAALKEFAFMKALEEHDFP 172
Cdd:cd05144    2 SSVGNQIGVGKESDVYLALDEDGNPVVLKFHRLGRTSFRKVKRKRDYLKHRKHASWLYLSRLAAEKEFAALKALYEEGFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 173 VPKAIDCNRHCVIMSLVQGYPMVQVKQLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDFPQMVSVS 252
Cdd:cd05144   82 VPKPIDWNRHAVVMELIDGYPLYQVRLLEDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEKITVIDFPQMVSTS 161

                        170       180
                 ....*....|....*....|..
gi 145339355 253 HRNAQMYFDRDIECIFKFFRKR 274
Cdd:cd05144  162 HPNAEEYFDRDVECIIKFFRRK 183
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 106-283 1.15e-72

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


Pssm-ID: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 227.12  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  106 DIFEVAQEDGTILAMKLHRLGRTSFRAVKSKRDYLRHR--SSFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCNRHC 183
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFrdRKTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNRHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  184 VIMSLV--QGYPMVQVKQLQ--NPETIFEKIIGIVVRL-AEHGLIHCDFNEFNIMIDDeEKITMIDFPQMVSVSHRNAQM 258
Cdd:pfam01163  81 LVMEFIgkDGVPAPKLKDVEleEAEEIYDEIIREMRRLyQEAGLVHGDLSEYNILVHD-DKPVIIDVPQAVETDHPNALE 159

                         170       180
                  ....*....|....*....|....*
gi 145339355  259 YFDRDIECIFKFFRKRFNMSFHEDK 283
Cdd:pfam01163 160 FLERDVENIINFFRRKGVDEVDERK 184
RIO smart00090
RIO-like kinase;
64-274 3.23e-55

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 183.66  E-value: 3.23e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355    64 DSSKYDGFRLTYLGYDFLAIKTLVNRGIFTGVGRQIGVGKESDIFEV--AQEDGTILAMKLHRLGRTSFRAVKSKRDYLR 141
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAldFDGSGKERAVKIYRTGTLEFKRRDRYVDGDF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355   142 --HRSSFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCNRHCVIMSLV--QGYPMVQVKQLQN----PETIFEKIIGI 213
Cdd:smart00090  81 rfKYRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIggDGLPAPRLKDVEPeeeeEFELYDDILEE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145339355   214 VVRLAEHG-LIHCDFNEFNIMIDDeEKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFFRKR 274
Cdd:smart00090 161 MRKLYKEGeLVHGDLSEYNILVHD-GKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRK 221
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 112-277 2.50e-52

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: 174.32  E-value: 2.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 112 QEDGTILAMKLHRLGRTSFRAVKSKRDYLRHrssFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCNRHCVIMSLVQG 191
Cdd:COG0478    5 SPGGGPVALKFHREGRTSFRKVRRERADKEH---YSWLYAARTRAEREFRALERLYPAGLPVPRPIAANRHAIVMERIEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 192 YPMVQVKqLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFF 271
Cdd:COG0478   82 VELARLK-LEDPEEVLDKILEEIRRAHDAGIVHADLSEYNILVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSF 160


                 ....*.
gi 145339355 272 RKRFNM 277
Cdd:COG0478  161 RKKYGL 166
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
81-274 2.92e-36

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


Pssm-ID: 441324  Cd Length: 252  Bit Score: 134.16  E-value: 2.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  81 LAIKTLVNRGIFTGVGRQIGVGKESDIFEVAQEDGTILAMKLHRLGRTSF-RAVK---------SKRDYLRHRSSFSWly 150
Cdd:COG1718   36 KALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTATSSFkRMAQyiegdprfmGKGSFGRRQLIFAW-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 151 lsrlaALKEFAFMKALEEHDFPVPKAIDCNRHCVIMSLV--QGYP---MVQVK-QLQNPETIFEKIIGIVVRLAEHGLIH 224
Cdd:COG1718  114 -----ARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIgdDGVPaprLKDVElEPEEAEELYEQLIEYIVRLYKAGLVH 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 145339355 225 CDFNEFNIMIDDEEkITMIDFPQMVSVSHRNAQMYFDRDIECIFKFFRKR 274
Cdd:COG1718  189 GDLSEYNILVDDGG-PVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
 8-89 2.32e-33

Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to the winged helix (wHTH) domain. They adopt a structure consisting of four alpha helices followed by two beta strands and a fifth alpha helix. The domain confers DNA binding properties to the protein, as per other winged helix domains.


Pssm-ID: 462715  Cd Length: 82  Bit Score: 120.73  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355    8 LRYLSKDDFRVLTAVEMGMRNHEIVPSELVERIACLKHGGTYKVLKNLLKYKLLHHDSSKYDGFRLTYLGYDFLAIKTLV 87
Cdd:pfam09202   1 MRYLSKEDFRVLTAVEMGMRNHEVVPTELITSISRLRHGGVNKRLSRLAKRKLISRKNAKYDGYRLTYLGYDYLALRTLV 80


                  ..
gi 145339355   88 NR 89
Cdd:pfam09202  81 KR 82
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 95-274 1.02e-28

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. 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 RIO 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: 270696 [Multi-domain]  Cd Length: 189  Bit Score: 111.49  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  95 VGRQIGVGKESDIFEVAQEDGTILAMKLHRLgRTSFRavKSKRDYLRHRSSFSWLYLSRLAAL------KEFAFMKALEE 168
Cdd:cd05145    1 LGGVISTGKEANVYLARGGDGEPVAVKIYRT-STSSF--KKMAKYIEGDPRFESRRRGNRRKLifawarKEFRNLKRLYE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 169 HDFPVPKAIDCNRHCVIMSLV--QGYPMVQVKQLQ----NPETIFEKIIGIVVRL-AEHGLIHCDFNEFNIMIDDEeKIT 241
Cdd:cd05145   78 AGVRVPEPIAVYRNVLVMEFIgdDGSPAPRLKDVEleeeDAEELYEQVVEQMRRMyCKAGLVHGDLSEYNILYYDG-KPV 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 145339355 242 MIDFPQMVSVSHRNAQMYFDRDIECIFKFFRKR 274
Cdd:cd05145  157 IIDVSQAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 95-273 2.07e-18

Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical protein serine kinases present in archaea, bacteria and eukaryotes. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. RIO kinases contain a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. Most organisms contain at least two RIO kinases, RIO1 and RIO2. A third protein, RIO3, is present in multicellular eukaryotes. In yeast, RIO1 and RIO2 are essential for survival. They function as non-ribosomal factors necessary for late 18S rRNA processing. RIO1 is also required for proper cell cycle progression and chromosome maintenance. The biological substrates for RIO kinases are still unknown. The RIO 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: 270689  Cd Length: 192  Bit Score: 83.15  E-value: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  95 VGRQIGVGKESDIFEVAQE-DGTILAM--KLHRLGRTSFRAVK------SKRDYlrHRSSFSWLYLsrLAALKEFAFMKA 165
Cdd:cd05119    1 IGGVISTGKEANVFYADGVfDGKPVACavKIYRIETSEFDKVDeylygdERFDY--RRISPKEKVF--IWTEKEFRNLER 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 166 LEEHDFPVPKAIDCNRHCVIMSLVQG--------YPMVQVKQLQNPETIFEKIIGIVVRL-AEHGLIHCDFNEFNIMIDD 236
Cdd:cd05119   77 AKEAGVSVPQPYTYEKNVLL*EFIGEdelpaptlVELGRELKELDVEGIFNDVVENVKRLyQEAELVHADLSEYNILYID 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145339355 237 eeKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFFRK 273
Cdd:cd05119  157 --KVYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 158-282 2.05e-11

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: 61.90  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 158 KEFAFMKALEEHDFPVPK--AIDCNRHCVIMSLVQGYPMVQV-KQLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMI 234
Cdd:COG3642    5 REARLLRELREAGVPVPKvlDVDPDDADLVMEYIEGETLADLlEEGELPPELLRELGRLLARLHRAGIVHGDLTTSNILV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145339355 235 DDeEKITMIDFPQMvsvSHRNAQMYFDRDIECIFKFFRKRFNMSFHED 282
Cdd:COG3642   85 DD-GGVYLIDFGLA---RYSDPLEDKAVDLAVLKRSLESTHPDPAEEL 128
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 140-245 6.36e-10

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 59.13  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 140 LRH-----------RSSFSWLYLSRLAALKEFAFMKALEEHDFPVPKAIDCN--RHCV------IMSLVQGypmVQ--VK 198
Cdd:PRK01723  60 LRHyrrggligklsKDRYLFTGLERTRAFAEFRLLAQLYEAGLPVPRPIAARvvRHGLfyradiLIERIEG---ARdlVA 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 145339355 199 QLQN---PETIFEKIIGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDF 245
Cdd:PRK01723 137 LLQEaplSEEQWQAIGQLIARFHDAGVYHADLNAHNILLDPDGKFWLIDF 186
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 99-274 4.62e-08

Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is present in archaea, bacteria and eukaryotes. This subfamily is composed of RIO1 proteins from eukaryotes. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. It is associated with precursors of 40S ribosomal subunits, just like RIO2. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. 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 RIO 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: 270698  Cd Length: 190  Bit Score: 52.96  E-value: 4.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  99 IGVGKESDIFEVAQEDGTILAMKLHRlgrTSFRAVKSKRDYL----RHRSSFS----------WlylsrlaALKEFAFMK 164
Cdd:cd05147    5 ISTGKEANVYHATTKNGGELAIKVYK---TSILVFKDRDKYVsgefRFRHGYCkhnprkmvktW-------AEKEMRNLK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 165 ALEEHDFPVPKAIDCNRHCVIMSLV--QGYPMVQVKQLQNPET----IFEKIIGIVVRLAEHG-LIHCDFNEFNIMIDDE 237
Cdd:cd05147   75 RLNQAGIPCPEPILLRSHVLVMEFIgkDGWPAPRLKDAKLSESkwreLYLQVIKIMRRMYQKCrLVHADLSEYNLLYHKG 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145339355 238 eKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFFRKR 274
Cdd:cd05147  155 -KVYIIDVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 99-274 4.38e-07

Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in multicellular eukaryotes. It is associated with precursors of 40S ribosomal subunits, just like RIO1 and RIO2. Its specific function is still unknown. Like RIO1 and RIO2, it may be involved in ribosomal subunit processing and 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 RIO3 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: 270697  Cd Length: 196  Bit Score: 50.06  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  99 IGVGKESDIFEVA--QEDGTIL----AMKLHRlgrTSFRAVKSKRDYL----RHRSSFSWL---YLSRLAALKEFAFMKA 165
Cdd:cd05146    5 ISTGKEAVVFHANggSMEEVLLppecAIKVFK---TTLNEFKNRDKYIkddyRFKDRFSKQnprKIIRLWAEKEMHNLKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 166 LEEHDFPVPKAIDCNRHCVIMSLVqGYPMVQVKQLQNP-------ETIFEKIIGIVVRL-AEHGLIHCDFNEFNIMIDdE 237
Cdd:cd05146   82 MQKAGIPCPEVVLLKKHVLVMSFI-GKDQVPAPKLKDAklssadlKLAYEQVVQMMKTMyNECHLVHADLSEYNILWH-E 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145339355 238 EKITMIDFPQMVSVSHRNAQMYFDRDIECIFKFFRKR 274
Cdd:cd05146  160 GKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 153-245 8.07e-07

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 48.21  E-value: 8.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 153 RLAALKEFAFMKALEEHDFPVPKAIDCNRHC----VIMSLVQGYPMVQVKQL-----QNPETIFEKIIGIVVRLAEHGLI 223
Cdd:cd13968   34 GEDLESEMDILRRLKGLELNIPKVLVTEDVDgpniLLMELVKGGTLIAYTQEeeldeKDVESIMYQLAECMRLLHSFHLI 113

                         90       100
                 ....*....|....*....|..
gi 145339355 224 HCDFNEFNIMIDDEEKITMIDF 245
Cdd:cd13968  114 HRDLNNDNILLSEDGNVKLIDF 135
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 158-245 9.68e-07

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK 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), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 48.45  E-value: 9.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 158 KEFAFMKALEEH-DFPVPKAIDCNRHC----VIMSLVQGYPMVQVKQLQNPETIfEKIIGivvRLAEH----------GL 222
Cdd:cd05120   38 KEAAMLQLLAGKlSLPVPKVYGFGESDgweyLLMERIEGETLSEVWPRLSEEEK-EKIAD---QLAEIlaalhridssVL 113

                         90       100
                 ....*....|....*....|....
gi 145339355 223 IHCDFNEFNIMIDDEEKIT-MIDF 245
Cdd:cd05120  114 THGDLHPGNILVKPDGKLSgIIDW 137
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
 173-261 5.24e-06

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 47.49  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 173 VPKAID--CNRHCVIMSLVQGYPMVQVKQLQ----NPETIFEKIIGIVVR-LAEHGLIHCDFNEFNIMIDDEEKITMIDF 245
Cdd:cd05121  135 VPKVYPelSTRRVLVMEYIDGVKLTDLEALRaagiDRKELARRLVDAYLKqIFEDGFFHADPHPGNILVLPDGRIALLDF 214

                         90
                 ....*....|....*.
gi 145339355 246 PQMVSVSHRNAQMYFD 261
Cdd:cd05121  215 GMVGRLDPETREALAD 230
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 97-245 1.33e-05

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 46.84  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  97 RQIGVGkESDIFEVAQEDGTILAMKLHRLGRTSFRAVKSkrdylrhrssfswlylsrlaalkEFAFMKALEEHDFPVPKA 176
Cdd:COG2334   19 KPLNSG-ENRNYRVETEDGRRYVLKLYRPGRWSPEEIPF-----------------------ELALLAHLAAAGLPVPAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 177 I----------DCNRHCVIMSLVQGYPM-------------------------------------VQVKQLQNPETIFEK 209
Cdd:COG2334   75 VptrdgetlleLEGRPAALFPFLPGRSPeepspeqleelgrllarlhraladfprpnardlawwdELLERLLGPLLPDPE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 145339355 210 IIGIVVRLAEH--------------GLIHCDFNEFNIMIDDEEKITMIDF 245
Cdd:COG2334  155 DRALLEELLDRlearlapllgalprGVIHGDLHPDNVLFDGDGVSGLIDF 204
lanthi_synth_III NF038151
class III lanthionine synthetase LanKC;
153-245 4.23e-05

class III lanthionine synthetase LanKC;


Pssm-ID: 468387 [Multi-domain]  Cd Length: 831  Bit Score: 46.01  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 153 RLAalKEFAFMKALEEHDFpVPKAIDCNR----HCVIMSLVQGYPMVQVKQLQNP------------------ETIFEKI 210
Cdd:NF038151 269 RLR--REREALERLAGLGG-VPEVIDYFTvwehHFLVEEFVEGRPLNSWLARRYPltradpdpealaaytewaLRILRQV 345

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145339355 211 IGIVVRLAEHGLIHCDFNEFNIMIDDEEKITMIDF 245
Cdd:NF038151 346 ERAVAAVHARGVVFGDLHPFNIMVDPDGSVRLIDF 380
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 110-245 9.91e-05

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 428872  Cd Length: 206  Bit Score: 43.53  E-value: 9.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  110 VAQEDGTILAMKLHRLGRTSfravKSKRDYLRHRssfswlyLSRLAALKEFAFMKALEEHDFPVPKAI-------DCNRH 182
Cdd:pfam06293  22 VVARVGNGVLRKYYRGGMWG----HLNRDLYRYP-------LGRTRAFREFRLIRRLREAGLPVPKPVaagevkvGGGYR 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145339355  183 CVIM--------SLVQGYPMVQVKQLQNPETIFEKIIGIVVRLAEHGLIHCDFNEFNIMID----DEEKITMIDF 245
Cdd:pfam06293  91 ADLLterlegaqSLADWLADWAVPSGELRRAIWEAVGRLIRQMHRAGVQHGDLYAHHILLQqegdEGFEAWLIDL 165
AarF COG0661
Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme ...
 155-245 6.73e-04

Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family [Coenzyme transport and metabolism, Signal transduction mechanisms]; Predicted protein kinase regulating ubiquinone biosynthesis, AarF/ABC1/UbiB family is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440425 [Multi-domain]  Cd Length: 487  Bit Score: 42.11  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 155 AALKEFAfmKALEEH-DFPVPKAID--CNRHCVIMSLVQGYPMVQVKQLQNPETIFEKIIGIVVR-----LAEHGLIHCD 226
Cdd:COG0661  207 ANAERFR--RNFADDpDVYVPKVYWelSTRRVLTMEWIDGIKISDLEALDAAGIDRKRLAERLVRaflrqVFRDGFFHAD 284

                         90
                 ....*....|....*....
gi 145339355 227 FNEFNIMIDDEEKITMIDF 245
Cdd:COG0661  285 PHPGNIFVLPDGRLVLLDF 303
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
95-245 1.25e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.15  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355  95 VGRQIGVGKESDIFEVAQEdgtilamklhRLGRTsfRAVKSkrdyLRHRSSFSWLYLSRLaaLKEFAFMKALEeHDFpVP 174
Cdd:COG0515   11 ILRLLGRGGMGVVYLARDL----------RLGRP--VALKV----LRPELAADPEARERF--RREARALARLN-HPN-IV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145339355 175 KAIDC----NRHCVIMSLVQGYPMVQVKQLQNPETIfEKIIGIVVRLAE-------HGLIHCDFNEFNIMIDDEEKITMI 243
Cdd:COG0515   71 RVYDVgeedGRPYLVMEYVEGESLADLLRRRGPLPP-AEALRILAQLAEalaaahaAGIVHRDIKPANILLTPDGRVKLI 149


                 ..
gi 145339355 244 DF 245
Cdd:COG0515  150 DF 151
 
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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