Protein Family Models for Protein (Select 692125012) - Protein Family Models

Select item 4153851.

Polyribonucleotide nucleotidyltransferase, RNA binding domain

This family contains the RNA binding domain of Polyribonucleotide nucleotidyltransferase (PNPase) PNPase is involved in mRNA degradation in a 3'-5' direction. (from Pfam)

GO Terms:

Molecular Function:: RNA binding (GO:0003723)

Biological Process:: RNA processing (GO:0006396)

Date:: 2024-08-14

Family Accession:: NF015671.5
Method:: HMM

Select item 4152092.

3' exoribonuclease family, domain 2

This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components, Swiss:P46948 Swiss:Q12277 and Swiss:P25359 contain a copy of this domain [1]. Swiss:Q10205, a hypothetical protein from S. pombe appears to belong to an uncharacterised subfamily. This subfamily is found in both eukaryotes and archaebacteria. [1]. 9390555. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases. Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D;. Cell 1997;91:457-466. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF015670.5
Method:: HMM

Select item 4118753.

KH domain-containing protein

KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia. [1]. 8036511. Conserved structures and diversity of functions of RNA-binding proteins. Burd CG, Dreyfuss G;. Science 1994;265:615-621. [2]. 8612276. Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A;. Cell 1996;85:237-245. (from Pfam)

GO Terms:

Molecular Function:: RNA binding (GO:0003723)

Date:: 2024-10-16

Family Accession:: NF012243.5
Method:: HMM

Select item 4111874.

3' exoribonuclease family, domain 1

This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components, Swiss:P46948 Swiss:Q12277 and Swiss:P25359 contain a copy of this domain [1]. Swiss:Q10205, a hypothetical protein from S. pombe appears to belong to an uncharacterised subfamily. This subfamily is found in both eukaryotes and archaebacteria. [1]. 9390555. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases. Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D;. Cell 1997;91:457-466. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF013318.5
Method:: HMM

Select item 4108415.

S1 RNA-binding domain-containing protein

The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure. Structure and an extension of S1 family. [1]. 9008164. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG;. Cell 1997;88:235-242. (from Pfam)

GO Terms:

Molecular Function:: nucleic acid binding (GO:0003676)

Date:: 2024-10-16

Family Accession:: NF012784.5
Method:: HMM

Select item 3930836.