NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|110622779|emb|CAJ38057|]
View 

predicted protein kinase [Methanocella arvoryzae MRE50]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RIO2 super family cl26665
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
5-291 7.92e-107

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


The actual alignment was detected with superfamily member COG0478:

Pssm-ID: 331486  Cd Length: 304  Bit Score: 316.57  E-value: 7.92e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779   5 AAVYLALVPNEKKVLRGVEEGMKRHEWVPVEDIEAYAGLGRKEVEYRLNRLVDMKIVERYIQSYAGYQLKFDGYDILAID 84
Cdd:COG0478    5 AEAYPKLSKEDFRLLRAIEGGMRSHEWVPLELIKKRARMDEEELLYRLKRLDKLKLVSRRTISYEGYQLTFSGYDALALH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  85 AFVKKETFGALGEVIGVGKESVVLAAMSHK--PVAVKFHREGRTSFKQVKRSRQHLVDIEivNFSWLYAAMLAAKREFEA 162
Cdd:COG0478   85 ALVKRGIVEAIGTKIGVGKESDVYVAIDPKgrKVAVKFHRLGRTSFRKVKRNRDYLADKE--HGSWLYVSRLAAEREFEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 163 MKILYP-AVSIPEPIDQNRHAIVMSVVKGIEMAKATLvDPEWY---LDSVIEQVKKAYELGIIHSDLSEFNIMVSDEG-L 237
Cdd:COG0478  163 LQRLYPeGVKVPKPIAWNRHAVVMEYIEGVELYRLRL-DVENPdeiLDKILEEVRKAYRRGIVHGDLSEFNILVTEDGdI 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110622779 238 TIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKKYRIRRDLQSTIGYIKGKESG 291
Cdd:COG0478  242 VVIDWPQAVPISHPDAEELLERDVENIIKYFRRKYGYKVEKEEELDRVREASEF 295
 
Name Accession Description Interval E-value
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
5-291 7.92e-107

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


Pssm-ID: 223554  Cd Length: 304  Bit Score: 316.57  E-value: 7.92e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779   5 AAVYLALVPNEKKVLRGVEEGMKRHEWVPVEDIEAYAGLGRKEVEYRLNRLVDMKIVERYIQSYAGYQLKFDGYDILAID 84
Cdd:COG0478    5 AEAYPKLSKEDFRLLRAIEGGMRSHEWVPLELIKKRARMDEEELLYRLKRLDKLKLVSRRTISYEGYQLTFSGYDALALH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  85 AFVKKETFGALGEVIGVGKESVVLAAMSHK--PVAVKFHREGRTSFKQVKRSRQHLVDIEivNFSWLYAAMLAAKREFEA 162
Cdd:COG0478   85 ALVKRGIVEAIGTKIGVGKESDVYVAIDPKgrKVAVKFHRLGRTSFRKVKRNRDYLADKE--HGSWLYVSRLAAEREFEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 163 MKILYP-AVSIPEPIDQNRHAIVMSVVKGIEMAKATLvDPEWY---LDSVIEQVKKAYELGIIHSDLSEFNIMVSDEG-L 237
Cdd:COG0478  163 LQRLYPeGVKVPKPIAWNRHAVVMEYIEGVELYRLRL-DVENPdeiLDKILEEVRKAYRRGIVHGDLSEFNILVTEDGdI 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110622779 238 TIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKKYRIRRDLQSTIGYIKGKESG 291
Cdd:COG0478  242 VVIDWPQAVPISHPDAEELLERDVENIIKYFRRKYGYKVEKEEELDRVREASEF 295
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
94-271 1.24e-77

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  Cd Length: 183  Bit Score: 237.79  E-value: 1.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  94 ALGEVIGVGKESVVLAAMSHK--PVAVKFHREGRTSFKQVKRSRQHLVDIEivNFSWLYAAMLAAKREFEAMKILYPA-V 170
Cdd:cd05144    3 SVGNQIGVGKESDVYLALDEDgnPVVLKFHRLGRTSFRKVKRKRDYLKHRK--HASWLYLSRLAAEKEFAALKALYEEgF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 171 SIPEPIDQNRHAIVMSVVKGIEMAKATLV-DPEWYLDSVIEQVKKAYELGIIHSDLSEFNIMVSDEG-LTIIDWPQYVKV 248
Cdd:cd05144   81 PVPKPIDWNRHAVVMELIDGYPLYQVRLLeDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEkITVIDFPQMVST 160
                        170       180
                 ....*....|....*....|...
gi 110622779 249 GSKTAEEMLERDVRNVLTHFEKK 271
Cdd:cd05144  161 SHPNAEEYFDRDVECIIKFFRRK 183
RIO smart00090
RIO-like kinase;
65-287 1.29e-54

RIO-like kinase;


Pssm-ID: 214511  Cd Length: 237  Bit Score: 180.19  E-value: 1.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779    65 IQSYAGYQLKFDGYDILAIDAFVKKETFGALGEVIGVGKESVVLAAM----SHKPVAVKFHREGRTSFKQVKRSRQHLVD 140
Cdd:smart00090   2 KEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALdfdgSGKERAVKIYRTGTLEFKRRDRYVDGDFR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779   141 IEIVNFSWLYAAMLAAKREFEAMKILYPA-VSIPEPIDQNRHAIVMSVVKGIEMAKATLVDPEW-------YLDSVIEQV 212
Cdd:smart00090  82 FKYRKINPRKLVRLWAEKEFRNLQRLYEAgVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPeeeeefeLYDDILEEM 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110622779   213 KKAYELG-IIHSDLSEFNIMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKKYRIRRDLQSTIGYIKG 287
Cdd:smart00090 162 RKLYKEGeLVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
114-272 2.07e-49

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: 307356  Cd Length: 185  Bit Score: 165.10  E-value: 2.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  114 KPVAVKFHREGRTSFKQVKRSRQHLVDIEIVNFSWLYAAMLAAKREFEAMKILYPA-VSIPEPIDQNRHAIVMSVV--KG 190
Cdd:pfam01163  11 KEVAVKIYRTGTTSFKKRKRYRSGDFRFRDRKTSWRYLVRLWAEKEFRNLKRLYEAgVPVPKPIDLNRHVLVMEFIgkDG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  191 IEMAK---ATLVDPEWYLDSVIEQVKKAY-ELGIIHSDLSEFNIMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLT 266
Cdd:pfam01163  91 VPAPKlkdVELEEAEEIYDEIIREMRRLYqEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPNALEFLERDVENIIN 170

                  ....*.
gi 110622779  267 HFEKKY 272
Cdd:pfam01163 171 FFRRKG 176
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
157-241 5.54e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749  Cd Length: 199  Bit Score: 46.05  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  157 KREFEAMKILYPA-VSIPEP--IDQNRHAIVMSVVKGIEMAKATLVDPEWYLDSVIEQVKKAYELGIIHSDLSEFNIMVS 233
Cdd:TIGR03724  45 RREARLLSRARKAgVNTPVIydVDPDNKTIVMEYIEGKPLKDVIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVR 124

                  ....*...
gi 110622779  234 DEGLTIID 241
Cdd:TIGR03724 125 DDKVYLID 132
PRK09605 PRK09605
bifunctional UGMP family protein/serine/threonine protein kinase; Validated
172-242 1.11e-05

bifunctional UGMP family protein/serine/threonine protein kinase; Validated


Pssm-ID: 236586  Cd Length: 535  Bit Score: 46.42  E-value: 1.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110622779 172 IPEP----IDQNRHAIVMSVVKGIEMAKATLVDPEwYLDSVIEQVKKAYELGIIHSDLSEFNIMVSDEGLTIIDW 242
Cdd:PRK09605 398 VPTPviydVDPEEKTIVMEYIGGKDLKDVLEGNPE-LVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDF 471
 
Name Accession Description Interval E-value
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
5-291 7.92e-107

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


Pssm-ID: 223554  Cd Length: 304  Bit Score: 316.57  E-value: 7.92e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779   5 AAVYLALVPNEKKVLRGVEEGMKRHEWVPVEDIEAYAGLGRKEVEYRLNRLVDMKIVERYIQSYAGYQLKFDGYDILAID 84
Cdd:COG0478    5 AEAYPKLSKEDFRLLRAIEGGMRSHEWVPLELIKKRARMDEEELLYRLKRLDKLKLVSRRTISYEGYQLTFSGYDALALH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  85 AFVKKETFGALGEVIGVGKESVVLAAMSHK--PVAVKFHREGRTSFKQVKRSRQHLVDIEivNFSWLYAAMLAAKREFEA 162
Cdd:COG0478   85 ALVKRGIVEAIGTKIGVGKESDVYVAIDPKgrKVAVKFHRLGRTSFRKVKRNRDYLADKE--HGSWLYVSRLAAEREFEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 163 MKILYP-AVSIPEPIDQNRHAIVMSVVKGIEMAKATLvDPEWY---LDSVIEQVKKAYELGIIHSDLSEFNIMVSDEG-L 237
Cdd:COG0478  163 LQRLYPeGVKVPKPIAWNRHAVVMEYIEGVELYRLRL-DVENPdeiLDKILEEVRKAYRRGIVHGDLSEFNILVTEDGdI 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110622779 238 TIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKKYRIRRDLQSTIGYIKGKESG 291
Cdd:COG0478  242 VVIDWPQAVPISHPDAEELLERDVENIIKYFRRKYGYKVEKEEELDRVREASEF 295
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
94-271 1.24e-77

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  Cd Length: 183  Bit Score: 237.79  E-value: 1.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  94 ALGEVIGVGKESVVLAAMSHK--PVAVKFHREGRTSFKQVKRSRQHLVDIEivNFSWLYAAMLAAKREFEAMKILYPA-V 170
Cdd:cd05144    3 SVGNQIGVGKESDVYLALDEDgnPVVLKFHRLGRTSFRKVKRKRDYLKHRK--HASWLYLSRLAAEKEFAALKALYEEgF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 171 SIPEPIDQNRHAIVMSVVKGIEMAKATLV-DPEWYLDSVIEQVKKAYELGIIHSDLSEFNIMVSDEG-LTIIDWPQYVKV 248
Cdd:cd05144   81 PVPKPIDWNRHAVVMELIDGYPLYQVRLLeDPEEVLDEILELIVKLAKHGLIHGDFSEFNILVDEDEkITVIDFPQMVST 160
                        170       180
                 ....*....|....*....|...
gi 110622779 249 GSKTAEEMLERDVRNVLTHFEKK 271
Cdd:cd05144  161 SHPNAEEYFDRDVECIIKFFRRK 183
RIO smart00090
RIO-like kinase;
65-287 1.29e-54

RIO-like kinase;


Pssm-ID: 214511  Cd Length: 237  Bit Score: 180.19  E-value: 1.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779    65 IQSYAGYQLKFDGYDILAIDAFVKKETFGALGEVIGVGKESVVLAAM----SHKPVAVKFHREGRTSFKQVKRSRQHLVD 140
Cdd:smart00090   2 KEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALdfdgSGKERAVKIYRTGTLEFKRRDRYVDGDFR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779   141 IEIVNFSWLYAAMLAAKREFEAMKILYPA-VSIPEPIDQNRHAIVMSVVKGIEMAKATLVDPEW-------YLDSVIEQV 212
Cdd:smart00090  82 FKYRKINPRKLVRLWAEKEFRNLQRLYEAgVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPeeeeefeLYDDILEEM 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110622779   213 KKAYELG-IIHSDLSEFNIMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKKYRIRRDLQSTIGYIKG 287
Cdd:smart00090 162 RKLYKEGeLVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
114-272 2.07e-49

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: 307356  Cd Length: 185  Bit Score: 165.10  E-value: 2.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  114 KPVAVKFHREGRTSFKQVKRSRQHLVDIEIVNFSWLYAAMLAAKREFEAMKILYPA-VSIPEPIDQNRHAIVMSVV--KG 190
Cdd:pfam01163  11 KEVAVKIYRTGTTSFKKRKRYRSGDFRFRDRKTSWRYLVRLWAEKEFRNLKRLYEAgVPVPKPIDLNRHVLVMEFIgkDG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  191 IEMAK---ATLVDPEWYLDSVIEQVKKAY-ELGIIHSDLSEFNIMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLT 266
Cdd:pfam01163  91 VPAPKlkdVELEEAEEIYDEIIREMRRLYqEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPNALEFLERDVENIIN 170

                  ....*.
gi 110622779  267 HFEKKY 272
Cdd:pfam01163 171 FFRRKG 176
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
45-291 9.41e-32

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


Pssm-ID: 224632  Cd Length: 268  Bit Score: 120.50  E-value: 9.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  45 RKEVEYRLNRLVDMKIVEryiqsyagyqLKFDGYDILAIDAFVKKETFGALGEVIGVGKESVVLAAMSH--KPVAVKFHR 122
Cdd:COG1718   12 ADKREKREKDKEDRKVVD----------EVFDKRTLETLRRLLSRGVITELVGCISTGKEANVYLAETGdgRYVAVKIYR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 123 EGRTSFKQVKRSRQ------HL-VDIEIVNFSWlyaamlaAKREFEAMKILYPA-VSIPEPIDQNRHAIVMSVVKGIEMA 194
Cdd:COG1718   82 TSTSEFKRIRRYIQgdprfrNSrSNRRKLVFAW-------ARKEFRNLKRAYEAgVRVPEPIAFRNNVLVMEFIGDDGLP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 195 KATLVD-------PEWYLDSVIEQVKKAY-ELGIIHSDLSEFNIMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLT 266
Cdd:COG1718  155 APRLKDvpleleeAEGLYEDVVEYMRRLYkEAGLVHGDLSEYNILVHDGEPYIIDVSQAVTIDHPNAFEFLERDVRNIAR 234
                        250       260
                 ....*....|....*....|....*
gi 110622779 267 HFEkKYRIRRDLQSTIGYIKGKESG 291
Cdd:COG1718  235 FFR-RKGVEADPEELLEEIKGRILG 258
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
95-271 8.14e-30

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  Cd Length: 189  Bit Score: 113.42  E-value: 8.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  95 LGEVIGVGKESVVLAAMS--HKPVAVKFHR-------------EGRTSFKQVKRS-RQHLVdieivnFSWlyaamlaAKR 158
Cdd:cd05145    1 LGGVISTGKEANVYLARGgdGEPVAVKIYRtstssfkkmakyiEGDPRFESRRRGnRRKLI------FAW-------ARK 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 159 EFEAMKILYPA-VSIPEPIDQNRHAIVMSVVKGIEMAKATLVD-------PEWYLDSVIEQVKKAY-ELGIIHSDLSEFN 229
Cdd:cd05145   68 EFRNLKRLYEAgVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDveleeedAEELYEQVVEQMRRMYcKAGLVHGDLSEYN 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 110622779 230 IMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKK 271
Cdd:cd05145  148 ILYYDGKPVIIDVSQAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
95-270 1.88e-28

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: 109.73  E-value: 1.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  95 LGEVIGVGKESVVLAAMS---HKPV--AVKFHREGRTSFKQVKRSRQHLVDIEIVNFSWLYAAMLAAKREFEAMKILYPA 169
Cdd:cd05119    1 IGGVISTGKEANVFYADGvfdGKPVacAVKIYRIETSEFDKVDEYLYGDERFDYRRISPKEKVFIWTEKEFRNLERAKEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 170 -VSIPEPIDQNRHAIVMSVVKGIEMAKATLV---------DPEWYLDSVIEQVKKAY-ELGIIHSDLSEFNIMVSDeGLT 238
Cdd:cd05119   81 gVSVPQPYTYEKNVLL*EFIGEDELPAPTLVelgrelkelDVEGIFNDVVENVKRLYqEAELVHADLSEYNILYID-KVY 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 110622779 239 IIDWPQYVKVGSKTAEEMLERDVRNVLTHFEK 270
Cdd:cd05119  160 FIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
Rio2_N pfam09202
Rio2, N-terminal; Members of this family are found in Rio2, and are structurally homologous to ...
11-89 3.87e-23

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: 312646  Cd Length: 82  Bit Score: 91.85  E-value: 3.87e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110622779   11 LVPNEKKVLRGVEEGMKRHEWVPVEDIEAYAGLGRKEVEYRLNRLVDMKIVERYIQSYAGYQLKFDGYDILAIDAFVKK 89
Cdd:pfam09202   4 LSKEDFRVLTAVEMGMRNHEWVPTELITSISRLRHGGVNKRLSRLLKRKLISRKNAKYDGYRLTYLGYDYLALRTLVKR 82
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
156-271 8.16e-09

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: 54.11  E-value: 8.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 156 AKREFEAMKILYPA-VSIPEPIDQNRHAIVMSVV-KGIEMA----KATLVDPEW---YLDsVIEQVKKAY-ELGIIHSDL 225
Cdd:cd05147   66 AEKEMRNLKRLNQAgIPCPEPILLRSHVLVMEFIgKDGWPAprlkDAKLSESKWrelYLQ-VIKIMRRMYqKCRLVHADL 144
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 110622779 226 SEFNIMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKK 271
Cdd:cd05147  145 SEYNLLYHKGKVYIIDVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
98-271 9.49e-09

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: 53.91  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  98 VIGVGKESVVLAAMSHK--------PVAVKFHREGRTSFKQVKR------------SRQHlvDIEIVNfswlyaaMLAAK 157
Cdd:cd05146    4 CISTGKEAVVFHANGGSmeevllppECAIKVFKTTLNEFKNRDKyikddyrfkdrfSKQN--PRKIIR-------LWAEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 158 REFEAMKILYPAVSIPEPIDQNRHAIVMSVV--KGIEMAK---ATLVDPEWYL--DSVIEQVKKAY-ELGIIHSDLSEFN 229
Cdd:cd05146   75 EMHNLKRMQKAGIPCPEVVLLKKHVLVMSFIgkDQVPAPKlkdAKLSSADLKLayEQVVQMMKTMYnECHLVHADLSEYN 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 110622779 230 IMVSDEGLTIIDWPQYVKVGSKTAEEMLERDVRNVLTHFEKK 271
Cdd:cd05146  155 ILWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
157-241 5.54e-06

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749  Cd Length: 199  Bit Score: 46.05  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  157 KREFEAMKILYPA-VSIPEP--IDQNRHAIVMSVVKGIEMAKATLVDPEWYLDSVIEQVKKAYELGIIHSDLSEFNIMVS 233
Cdd:TIGR03724  45 RREARLLSRARKAgVNTPVIydVDPDNKTIVMEYIEGKPLKDVIEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIVR 124

                  ....*...
gi 110622779  234 DEGLTIID 241
Cdd:TIGR03724 125 DDKVYLID 132
PRK09605 PRK09605
bifunctional UGMP family protein/serine/threonine protein kinase; Validated
172-242 1.11e-05

bifunctional UGMP family protein/serine/threonine protein kinase; Validated


Pssm-ID: 236586  Cd Length: 535  Bit Score: 46.42  E-value: 1.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110622779 172 IPEP----IDQNRHAIVMSVVKGIEMAKATLVDPEwYLDSVIEQVKKAYELGIIHSDLSEFNIMVSDEGLTIIDW 242
Cdd:PRK09605 398 VPTPviydVDPEEKTIVMEYIGGKDLKDVLEGNPE-LVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDF 471
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
157-241 8.70e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168  Cd Length: 204  Bit Score: 42.65  E-value: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 157 KREFEAMKILYpAVSIPEP----IDQNRHAIVMSVVKGiEMAKATLVDPEW-YLDSVIEQVKKAYELGIIHSDLSEFNIM 231
Cdd:COG3642   47 RREARILAKAR-EAGVPVPivydVDPDNGLIVMEYIEG-ELLKDALEEARPdLLREVGRLVGKLHKAGIVHGDLTTSNII 124
                         90
                 ....*....|
gi 110622779 232 VSDEGLTIID 241
Cdd:COG3642  125 LSGGRIYFID 134
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
157-241 9.96e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 42.59  E-value: 9.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 157 KREFEAMKILYPA-VSIPEP--IDQNRHAIVMSVVKGIEMAkaTLVDPE-----WYLDSVIEQVKKAYELGIIHSDLSEF 228
Cdd:PRK14879  47 RREARIMSRARKAgVNVPAVyfVDPENFIIVMEYIEGEPLK--DLINSNgmeelELSREIGRLVGKLHSAGIIHGDLTTS 124
                         90
                 ....*....|...
gi 110622779 229 NIMVSDEGLTIID 241
Cdd:PRK14879 125 NMILSGGKIYLID 137
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
157-242 3.09e-04

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily 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: 270700  Cd Length: 152  Bit Score: 40.23  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 157 KREFEAMKILYPA-VSiPEPI--DQNRHAIVMSVVKGIEMAKATLVDPEwYLDSVIEQVKKAYELGII-----HSDLSEF 228
Cdd:cd05151   40 ENEKANSKAAAELgIA-PEVIyfDPETGVKITEFIEGATLLTNDFSDPE-NLERIAALLRKLHSSPLEdlvlcHNDLVPG 117
                         90
                 ....*....|....
gi 110622779 229 NIMVSDEGLTIIDW 242
Cdd:cd05151  118 NFLLDDDRLYLIDW 131
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
158-241 4.62e-04

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  Cd Length: 136  Bit Score: 39.35  E-value: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 158 REFEAMKILY-PAVSIPEPIDQNRHA----IVMSVVKGIEMAKATL------VDPEWYLDSVIEQVKKAYELGIIHSDLS 226
Cdd:cd13968   39 SEMDILRRLKgLELNIPKVLVTEDVDgpniLLMELVKGGTLIAYTQeeeldeKDVESIMYQLAECMRLLHSFHLIHRDLN 118
                         90
                 ....*....|....*.
gi 110622779 227 EFNIMVSDEG-LTIID 241
Cdd:cd13968  119 NDNILLSEDGnVKLID 134
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
157-242 1.64e-03

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  Cd Length: 158  Bit Score: 38.05  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 157 KREFEAMKIL--YPAVSIPEPI----DQNRHAIVMSVVKGiemakaTLVDPEWYLDSVIEQVKKAYELG----------- 219
Cdd:cd05120   37 EKEAAMLQLLagKLSLPVPKVYgfgeSDGWEYLLMERIEG------ETLSEVWPRLSEEEKEKIADQLAeilaalhrids 110
                         90       100
                 ....*....|....*....|....*..
gi 110622779 220 --IIHSDLSEFNIMVSDEG--LTIIDW 242
Cdd:cd05120  111 svLTHGDLHPGNILVKPDGklSGIIDW 137
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
95-241 8.83e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 37.03  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779  95 LGEVIGVGKESVVLAAMSHKPVAVKFHREGRTSFKQVKRSrqhlvdieivnfswlyaamlaAKREFEAMKILYPAVSIPE 174
Cdd:COG0515    4 ILRKLGEGSFGEVYLARDRKLVALKVLAKKLESKSKEVER---------------------FLREIQILASLNHPPNIVK 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622779 175 PID----QNRHAIVMSVVKG------IEMAKATLVDPEWYLDSVIEQVKKA----YELGIIHSDLSEFNIMVSDEG--LT 238
Cdd:COG0515   63 LYDffqdEGSLYLVMEYVDGgsledlLKKIGRKGPLSESEALFILAQILSAleylHSKGIIHRDIKPENILLDRDGrvVK 142

                 ...
gi 110622779 239 IID 241
Cdd:COG0515  143 LID 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH