ID A0A0D3A6C1_BRAOL Unreviewed; 200 AA.
AC A0A0D3A6C1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pre-mRNA cleavage factor Im 25 kDa subunit {ECO:0000256|PIRNR:PIRNR017888};
GN Name=106343002 {ECO:0000313|EnsemblPlants:Bo1g040290.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g040290.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g040290.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g040290.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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}.
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DR RefSeq; XP_013637552.1; XM_013782098.1.
DR AlphaFoldDB; A0A0D3A6C1; -.
DR STRING; 109376.A0A0D3A6C1; -.
DR EnsemblPlants; Bo1g040290.1; Bo1g040290.1; Bo1g040290.
DR GeneID; 106343002; -.
DR Gramene; Bo1g040290.1; Bo1g040290.1; Bo1g040290.
DR KEGG; boe:106343002; -.
DR eggNOG; KOG1689; Eukaryota.
DR HOGENOM; CLU_068704_1_1_1; -.
DR OMA; QCMREEF; -.
DR OrthoDB; 142507at2759; -.
DR Proteomes; UP000032141; Chromosome C1.
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:UP000032141};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017888}.
SQ SEQUENCE 200 AA; 22885 MW; A9ECE5313B21C435 CRC64;
MAMSQIVNTY PLSNYSFGTK EPKLEKDTSV ADRLARMKIN YMKEGMRTSV DAILLVQEHN
HPHILLLQIG NTFCKLPGGR LKPGENEVEG LKRKLTSKLG GNSAGLVPDW KVGECVATWW
RPNFETMMYP YCPPHITKPK ECKRLYVVHL SEKEYFAVPK NLKLLAVPLF ELYDNVQRYG
PVISTIPQQL SRFHFNMISS
//