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Conserved domains on  [gi|2462561881|ref|XP_054175290|]
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serine/threonine-protein kinase RIO3 isoform X3 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 69-197 4.72e-85

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05146:

Pssm-ID: 473864  Cd Length: 196  Bit Score: 252.29  E-value: 4.72e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  69 RKIVKLY----LQNVpSRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHEC 144
Cdd:cd05146    65 RKIIRLWaekeMHNL-KRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNEC 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462561881 145 TLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 197
Cdd:cd05146   144 HLVHADLSEYNILWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
 
Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 69-197 4.72e-85

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: 252.29  E-value: 4.72e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  69 RKIVKLY----LQNVpSRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHEC 144
Cdd:cd05146    65 RKIIRLWaekeMHNL-KRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNEC 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462561881 145 TLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 197
Cdd:cd05146   144 HLVHADLSEYNILWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
69-214 1.02e-68

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 212.16  E-value: 1.02e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881   69 RKIVKLY----LQNVpSRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHEC 144
Cdd:smart00090  90 RKLVRLWaekeFRNL-QRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDILEEMRKLYKEG 168

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  145 TLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERELFNAVSG 214
Cdd:smart00090 169 ELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE-LDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 81-207 1.11e-60

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: 189.75  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLnsEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHA 160
Cdd:pfam01163  61 KRLYEAGVPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHD 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462561881 161 GKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERE 207
Cdd:pfam01163 139 DKPVIIDVPQAVETDHPNALEFLERDVENIINFFRRKGVDE-VDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
81-212 6.79e-46

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 154.19  E-value: 6.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYhECTLVHADLSEYNMLWHA 160
Cdd:COG1718   122 YRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDD 200

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462561881 161 GKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKeaLSERELFNAV 212
Cdd:COG1718   201 GGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPE--LDPEELLKEI 250
PRK14879 PRK14879
Kae1-associated kinase Bud32;
81-185 9.65e-09

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 54.14  E-value: 9.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKEVkLNSEEMKEA-YYQTLHLMRQLYHECTLVHADLSEYNML 157
Cdd:PRK14879   54 SRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKDL-INSNGMEELeLSREIGRLVGKLHSAGIIHGDLTTSNMI 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462561881 158 WHAGKVWLID-----VSQSVEP--------------THPHGLEFLFR 185
Cdd:PRK14879  128 LSGGKIYLIDfglaeFSKDLEDravdlhvllrslesTHPDWAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 81-174 3.99e-07

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 [Multi-domain]  Cd Length: 199  Bit Score: 49.13  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEVklnSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLW 158
Cdd:TIGR03724  52 SRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDV---IEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIV 123

                          90       100
                  ....*....|....*....|.
gi 2462561881 159 HAGKVWLID-----VSQSVEP 174
Cdd:TIGR03724 124 RDDKVYLIDfglgkYSDEIED 144
 
Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 69-197 4.72e-85

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: 252.29  E-value: 4.72e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  69 RKIVKLY----LQNVpSRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHEC 144
Cdd:cd05146    65 RKIIRLWaekeMHNL-KRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNEC 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462561881 145 TLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 197
Cdd:cd05146   144 HLVHADLSEYNILWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
69-214 1.02e-68

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 212.16  E-value: 1.02e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881   69 RKIVKLY----LQNVpSRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHEC 144
Cdd:smart00090  90 RKLVRLWaekeFRNL-QRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDILEEMRKLYKEG 168

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  145 TLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERELFNAVSG 214
Cdd:smart00090 169 ELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE-LDEEELFERITG 237
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 43-196 1.13e-67

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: 207.81  E-value: 1.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  43 RQSLAVLVQERSLLSFM----HMEGAWRMK--------RKIVKLY----LQNVpSRMQRAGIPCPTVVLLKKHILVMSFI 106
Cdd:cd05147    21 GGELAIKVYKTSILVFKdrdkYVSGEFRFRhgyckhnpRKMVKTWaekeMRNL-KRLNQAGIPCPEPILLRSHVLVMEFI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881 107 GHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRD 186
Cdd:cd05147   100 GKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIIDVSQSVEHDHPHALEFLRRD 179

                         170
                  ....*....|
gi 2462561881 187 CRNVSQFFQK 196
Cdd:cd05147   180 CVNVNDFFRK 189
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 81-196 1.62e-62

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: 194.69  E-value: 1.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHA 160
Cdd:cd05145    73 KRLYEAGVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNILYYD 152

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462561881 161 GKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 196
Cdd:cd05145   153 GKPVIIDVSQAVTLDHPNAEEFLRRDIRNINRFFSR 188
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 81-207 1.11e-60

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: 189.75  E-value: 1.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLnsEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHA 160
Cdd:pfam01163  61 KRLYEAGVPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHD 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462561881 161 GKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERE 207
Cdd:pfam01163 139 DKPVIIDVPQAVETDHPNALEFLERDVENIINFFRRKGVDE-VDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
81-212 6.79e-46

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 154.19  E-value: 6.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYhECTLVHADLSEYNMLWHA 160
Cdd:COG1718   122 YRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDD 200

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462561881 161 GKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKeaLSERELFNAV 212
Cdd:COG1718   201 GGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPE--LDPEELLKEI 250
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 82-196 6.37e-22

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: 90.08  E-value: 6.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  82 RMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVK--LNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWh 159
Cdd:cd05119    76 RAKEAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELGreLKELDVEGIFNDVVENVKRLYQEAELVHADLSEYNILY- 154

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462561881 160 AGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 196
Cdd:cd05119   155 IDKVYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 87-196 2.18e-19

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: 82.94  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  87 GIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLNsEEMKEAYYQTLHLMRQLYhECTLVHADLSEYN-MLWHAGKVWL 165
Cdd:cd05144    79 GFPVPKPIDWNRHAVVMELI-----DGYPLYQVRLL-EDPEEVLDEILELIVKLA-KHGLIHGDFSEFNiLVDEDEKITV 151

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462561881 166 IDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 196
Cdd:cd05144   152 IDFPQMVSTSHPNAEEYFDRDVECIIKFFRR 182
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 82-196 2.49e-19

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: 82.65  E-value: 2.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  82 RMQRAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLNSEEmkEAYYQTLHLMRQLyHECTLVHADLSEYN-MLWHA 160
Cdd:COG0478    55 RLYPAGLPVPRPIAANRHAIVMERI-----EGVELARLKLEDPE--EVLDKILEEIRRA-HDAGIVHADLSEYNiLVDDD 126

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462561881 161 GKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 196
Cdd:COG0478   127 GGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFRK 162
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 81-171 3.74e-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: 59.97  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVLLKKH--ILVMSFIghdqvPAPKLKEVKLNSEEMKEAYYQTLHLMRQLyHECTLVHADLSEYNMLW 158
Cdd:COG3642    11 RELREAGVPVPKVLDVDPDdaDLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARL-HRAGIVHGDLTTSNILV 84

                          90
                  ....*....|...
gi 2462561881 159 HAGKVWLIDVSQS 171
Cdd:COG3642    85 DDGGVYLIDFGLA 97
PRK14879 PRK14879
Kae1-associated kinase Bud32;
81-185 9.65e-09

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 54.14  E-value: 9.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKEVkLNSEEMKEA-YYQTLHLMRQLYHECTLVHADLSEYNML 157
Cdd:PRK14879   54 SRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKDL-INSNGMEELeLSREIGRLVGKLHSAGIIHGDLTTSNMI 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462561881 158 WHAGKVWLID-----VSQSVEP--------------THPHGLEFLFR 185
Cdd:PRK14879  128 LSGGKIYLIDfglaeFSKDLEDravdlhvllrslesTHPDWAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 81-174 3.99e-07

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 [Multi-domain]  Cd Length: 199  Bit Score: 49.13  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEVklnSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLW 158
Cdd:TIGR03724  52 SRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDV---IEENGDELAREIGRLVGKLHKAGIVHGDLTTSNIIV 123

                          90       100
                  ....*....|....*....|.
gi 2462561881 159 HAGKVWLID-----VSQSVEP 174
Cdd:TIGR03724 124 RDDKVYLIDfglgkYSDEIED 144
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
81-173 4.21e-06

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 47.58  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIPCPTV--VLLKKHILVMSFIGhdqvpAPKLKEVKLNSEEMKEAYYQTLHLMrqlyHECTLVHADLSEYNMLW 158
Cdd:PRK09605  391 SEARRAGVPTPVIydVDPEEKTIVMEYIG-----GKDLKDVLEGNPELVRKVGEIVAKL----HKAGIVHGDLTTSNFIV 461

                          90       100
                  ....*....|....*....|
gi 2462561881 159 HAGKVWLID-----VSQSVE 173
Cdd:PRK09605  462 RDDRLYLIDfglgkYSDLIE 481
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 83-167 6.88e-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 [Multi-domain]  Cd Length: 136  Bit Score: 38.96  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  83 MQRAGIPCPTVVLLK-------KHILVMSFIGHDQVPAPkLKEVKLNSEEMKEAYYQTLHLMRQLyHECTLVHADLSEYN 155
Cdd:cd13968    44 LRRLKGLELNIPKVLvtedvdgPNILLMELVKGGTLIAY-TQEEELDEKDVESIMYQLAECMRLL-HSFHLIHRDLNNDN 121

                          90
                  ....*....|...
gi 2462561881 156 -MLWHAGKVWLID 167
Cdd:cd13968   122 iLLSEDGNVKLID 134
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 81-167 2.47e-03

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 [Multi-domain]  Cd Length: 152  Bit Score: 37.53  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  81 SRMQRAGIpCPTVVLL--KKHILVMSFIghdqVPAPKLKEVKLNSEEMKEAyyqtLHLMRQLYH----ECTLVHADLSEY 154
Cdd:cd05151    47 KAAAELGI-APEVIYFdpETGVKITEFI----EGATLLTNDFSDPENLERI----AALLRKLHSspleDLVLCHNDLVPG 117

                          90
                  ....*....|...
gi 2462561881 155 NMLWHAGKVWLID 167
Cdd:cd05151   118 NFLLDDDRLYLID 130
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 127-167 3.87e-03

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


Pssm-ID: 234975  Cd Length: 239  Bit Score: 37.56  E-value: 3.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462561881 127 KEAYYQTLHLMRQLyHECTLVHADLSEYNMLW-HAGKVWLID 167
Cdd:PRK01723  145 EEQWQAIGQLIARF-HDAGVYHADLNAHNILLdPDGKFWLID 185
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 82-191 8.67e-03

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: 36.60  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462561881  82 RMQRAGIPCPTVV--------LLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSE 153
Cdd:pfam06293  66 RLREAGLPVPKPVaagevkvgGGYRADLLTERLEGAQSLADWLADWAVPSGELRRAIWEAVGRLIRQMHRAGVQHGDLYA 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462561881 154 YNMLWHAG-----KVWLIDVSQSVEPTHP-----HGLEFLFRDCRNVS 191
Cdd:pfam06293 146 HHILLQQEgdegfEAWLIDLDKGRLRLPArrwrnKDLARLLRSFLNIG 193
 
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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