RNA 3'-terminal phosphate cyclase-like protein (RCL1) plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1, and A2 that are required for proper maturation of the 18S RNA
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not ...
8-371
0e+00
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not RNA 3'-phosphate cyclase (6.5.1.4), but rather a homolog with a distinct function, found in the nucleolus and required for ribosomal RNA processing. Homo sapiens has both a member of this RCL (RNA terminal phosphate cyclase like) family and EC 6.5.1.4, while Saccharomyces has a member of this family only.
:
Pssm-ID: 274564 [Multi-domain] Cd Length: 360 Bit Score: 584.57 E-value: 0e+00
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not ...
8-371
0e+00
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not RNA 3'-phosphate cyclase (6.5.1.4), but rather a homolog with a distinct function, found in the nucleolus and required for ribosomal RNA processing. Homo sapiens has both a member of this RCL (RNA terminal phosphate cyclase like) family and EC 6.5.1.4, while Saccharomyces has a member of this family only.
Pssm-ID: 274564 [Multi-domain] Cd Length: 360 Bit Score: 584.57 E-value: 0e+00
RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded ...
4-343
0e+00
RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded in eukaryotic genomes. They lack a conserved catalytic histidine residue required for cyclase activity, so probably do not function as cyclases. They are believed to play a role in ribosomal RNA processing and assembly.
Pssm-ID: 238447 [Multi-domain] Cd Length: 341 Bit Score: 543.83 E-value: 0e+00
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are ...
12-341
1.04e-118
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.
Pssm-ID: 460079 [Multi-domain] Cd Length: 324 Bit Score: 346.81 E-value: 1.04e-118
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not ...
8-371
0e+00
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not RNA 3'-phosphate cyclase (6.5.1.4), but rather a homolog with a distinct function, found in the nucleolus and required for ribosomal RNA processing. Homo sapiens has both a member of this RCL (RNA terminal phosphate cyclase like) family and EC 6.5.1.4, while Saccharomyces has a member of this family only.
Pssm-ID: 274564 [Multi-domain] Cd Length: 360 Bit Score: 584.57 E-value: 0e+00
RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded ...
4-343
0e+00
RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded in eukaryotic genomes. They lack a conserved catalytic histidine residue required for cyclase activity, so probably do not function as cyclases. They are believed to play a role in ribosomal RNA processing and assembly.
Pssm-ID: 238447 [Multi-domain] Cd Length: 341 Bit Score: 543.83 E-value: 0e+00
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are ...
12-341
1.04e-118
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.
Pssm-ID: 460079 [Multi-domain] Cd Length: 324 Bit Score: 346.81 E-value: 1.04e-118
RNA 3' phosphate cyclase domain - RNA phosphate cyclases are enzymes that catalyze the ...
10-341
9.61e-79
RNA 3' phosphate cyclase domain - RNA phosphate cyclases are enzymes that catalyze the ATP-dependent conversion of 3'-phosphate at the end of RNA into 2', 3'-cyclic phosphodiester bond. The enzymes are conserved in eucaryotes, bacteria and archaea. The exact biological role of this enzyme is unknown, but it has been proposed that it is likely to function in cellular RNA metabolism and processing. RNA phosphate cyclase has been characterized in human (with at least three isozymes), and E. coli, and it seems to be taxonomically widespread. The crystal structure of RNA phospate cyclase shows that it consists of two domains. The larger domain contains three repeats of a fold originally identified in the bacterial translation initiation factor IF3.
Pssm-ID: 238183 [Multi-domain] Cd Length: 338 Bit Score: 245.34 E-value: 9.61e-79
RNA 3'-terminal phosphate cyclase (RTC), insert domain; RNA cyclases are a family of ...
183-288
6.12e-43
RNA 3'-terminal phosphate cyclase (RTC), insert domain; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.
Pssm-ID: 461577 [Multi-domain] Cd Length: 102 Bit Score: 144.62 E-value: 6.12e-43
RNA 3'-phosphate cyclase; Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4) ...
16-324
1.78e-34
RNA 3'-phosphate cyclase; Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4), an enzyme whose function is conserved from E. coli to human. The modification this enzyme performs enables certain RNA ligations to occur, although the full biological roll for this enzyme is not fully described. This model separates this enzyme from a related protein, present only in eukaryotes, localized to the nucleolus, and involved in ribosomal modification. [Transcription, RNA processing]
Pssm-ID: 274563 [Multi-domain] Cd Length: 326 Bit Score: 129.32 E-value: 1.78e-34
RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze ...
16-342
7.46e-33
RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze the ATP-dependent conversion of 3'-phosphate to a 2'.3'-cyclic phosphodiester at the end of RNA molecule. A conserved catalytic histidine residue is found in all members of this subfamily.
Pssm-ID: 238446 [Multi-domain] Cd Length: 326 Bit Score: 125.02 E-value: 7.46e-33
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
9-185
1.69e-30
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.
Pssm-ID: 238794 Cd Length: 211 Bit Score: 115.84 E-value: 1.69e-30
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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