LD24837p [Drosophila melanogaster]
Protein Classification
serine/threonine-protein kinase RIO1( domain architecture ID 10142323)
serine/threonine protein kinase RIO1 is an atypical protein kinase that catalyzes the ATP-dependent phosphorylation of serine residues in substrate proteins; it acts predominantly as an ATPase and is required for 18S rRNA processing, ribosome assembly, proper cell cycle progression, and chromosome maintenance
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| RIO1_euk | cd05147 | Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ... |
205-395 | 2.61e-143 | ||||
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: 411.96 E-value: 2.61e-143
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| Name | Accession | Description | Interval | E-value | |||||
| RIO1_euk | cd05147 | Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ... |
205-395 | 2.61e-143 | |||||
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: 411.96 E-value: 2.61e-143
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| RIO | smart00090 | RIO-like kinase; |
174-411 | 2.71e-111 | |||||
RIO-like kinase; Pssm-ID: 214511 [Multi-domain] Cd Length: 237 Bit Score: 332.34 E-value: 2.71e-111
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| RIO1 | pfam01163 | RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ... |
216-404 | 3.92e-97 | |||||
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: 293.76 E-value: 3.92e-97
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| RIO1 | COG1718 | Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms]; |
153-410 | 1.71e-80 | |||||
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms]; Pssm-ID: 441324 Cd Length: 252 Bit Score: 253.19 E-value: 1.71e-80
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| PRK14879 | PRK14879 | Kae1-associated kinase Bud32; |
209-371 | 1.46e-03 | |||||
Kae1-associated kinase Bud32; Pssm-ID: 237847 [Multi-domain] Cd Length: 211 Bit Score: 40.28 E-value: 1.46e-03
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| Name | Accession | Description | Interval | E-value | |||||
| RIO1_euk | cd05147 | Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ... |
205-395 | 2.61e-143 | |||||
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: 411.96 E-value: 2.61e-143
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| RIO | smart00090 | RIO-like kinase; |
174-411 | 2.71e-111 | |||||
RIO-like kinase; Pssm-ID: 214511 [Multi-domain] Cd Length: 237 Bit Score: 332.34 E-value: 2.71e-111
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| RIO1 | pfam01163 | RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ... |
216-404 | 3.92e-97 | |||||
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: 293.76 E-value: 3.92e-97
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| RIO1_like | cd05145 | Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ... |
205-395 | 6.39e-93 | |||||
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: 283.29 E-value: 6.39e-93
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| RIO3_euk | cd05146 | Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ... |
205-395 | 2.09e-89 | |||||
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: 274.24 E-value: 2.09e-89
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| RIO1 | COG1718 | Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms]; |
153-410 | 1.71e-80 | |||||
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms]; Pssm-ID: 441324 Cd Length: 252 Bit Score: 253.19 E-value: 1.71e-80
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| RIO | cd05119 | Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ... |
205-394 | 6.28e-30 | |||||
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: 116.28 E-value: 6.28e-30
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| RIO2_C | cd05144 | C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ... |
209-395 | 2.99e-28 | |||||
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: 111.44 E-value: 2.99e-28
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| RIO2 | COG0478 | RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ... |
268-411 | 2.58e-23 | |||||
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: 97.28 E-value: 2.58e-23
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| Bud32 | COG3642 | tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ... |
268-375 | 9.02e-09 | |||||
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: 54.58 E-value: 9.02e-09
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| PKc_like | cd13968 | Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ... |
209-365 | 1.69e-08 | |||||
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: 53.21 E-value: 1.69e-08
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| PRK14879 | PRK14879 | Kae1-associated kinase Bud32; |
209-371 | 1.46e-03 | |||||
Kae1-associated kinase Bud32; Pssm-ID: 237847 [Multi-domain] Cd Length: 211 Bit Score: 40.28 E-value: 1.46e-03
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| ABC1_ADCK3-like | cd05121 | Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ... |
217-365 | 7.68e-03 | |||||
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: 38.25 E-value: 7.68e-03
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