ID D8TUC5_VOLCA Unreviewed; 232 AA.
AC D8TUC5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Pre-mRNA cleavage factor Im 25 kDa subunit {ECO:0000256|PIRNR:PIRNR017888};
GN ORFNames=VOLCADRAFT_59795 {ECO:0000313|EMBL:EFJ49120.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ49120.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that plays
CC a key role in pre-mRNA 3'-processing. {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBUNIT: Homodimer. Component of the cleavage factor Im (CFIm) complex.
CC {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR017888}. Note=In
CC punctate subnuclear structures localized adjacent to nuclear speckles,
CC called paraspeckles. {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000256|ARBA:ARBA00009710, ECO:0000256|PIRNR:PIRNR017888}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL378337; EFJ49120.1; -; Genomic_DNA.
DR RefSeq; XP_002950017.1; XM_002949971.1.
DR AlphaFoldDB; D8TUC5; -.
DR STRING; 3068.D8TUC5; -.
DR GeneID; 9619337; -.
DR KEGG; vcn:VOLCADRAFT_59795; -.
DR eggNOG; KOG1689; Eukaryota.
DR InParanoid; D8TUC5; -.
DR OrthoDB; 142507at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR PANTHER; PTHR13047:SF0; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 5; 1.
DR PANTHER; PTHR13047; PRE-MRNA CLEAVAGE FACTOR IM, 25KD SUBUNIT; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR SUPFAM; SSF55811; Nudix; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR017888};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR017888};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017888}.
FT REGION 206..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 232 AA; 26696 MW; 8980A230848DBB08 CRC64;
MSSRGQPVFN VYPVGNYSFG TKAPKLEKDS NVNERLSRLK ANYEKEGMRR SAEAILLVQE
HNHPHVLLFQ LGQSFFRLPG GRLRPGEDEV EGLRRKLSNR LAPTNAALQV VWDVGEVLSV
FYRPNFDTMF YPYVPPHITR PKECRKLFVV QLPERCVFAV PKNMKLVAVP VFELYDNIPR
YGPIISSLPA VLSRLRLNLQ FVLPPPPPQQ QQQQQQHNGY GQQQQQEQHF PP
//