ID SEN2_SCHPO Reviewed; 380 AA. AC Q8TFH7; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Probable tRNA-splicing endonuclease subunit sen2; DE EC=4.6.1.16; DE AltName: Full=tRNA-intron endonuclease sen2; GN Name=sen2; ORFNames=SPAPB17E12.07c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Constitutes one of the two catalytic subunit of the tRNA- CC splicing endonuclease complex, a complex responsible for identification CC and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at CC the 5'- and 3'-splice sites to release the intron. The products are an CC intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and CC 5'-OH termini. There are no conserved sequences at the splice sites, CC but the intron is invariably located at the same site in the gene, CC placing the splice sites an invariant distance from the constant CC structural features of the tRNA body. This subunit may anchor the CC endonuclease complex to the nuclear membrane. Probably carries the CC active site for 5'-splice site cleavage (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'- CC half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with CC a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16; CC -!- SUBUNIT: Heterotetramer composed of sen2, sen15, sen34 and sen54. CC Interacts directly with sen54 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. CC {ECO:0000305}. 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; CU329670; CAD27500.1; -; Genomic_DNA. DR RefSeq; NP_001018222.1; NM_001018702.2. DR AlphaFoldDB; Q8TFH7; -. DR SMR; Q8TFH7; -. DR BioGRID; 280474; 1. DR STRING; 284812.Q8TFH7; -. DR MaxQB; Q8TFH7; -. DR PaxDb; 4896-SPAPB17E12-07c-1; -. DR EnsemblFungi; SPAPB17E12.07c.1; SPAPB17E12.07c.1:pep; SPAPB17E12.07c. DR GeneID; 3361398; -. DR KEGG; spo:SPAPB17E12.07c; -. DR PomBase; SPAPB17E12.07c; sen2. DR VEuPathDB; FungiDB:SPAPB17E12.07c; -. DR eggNOG; KOG4685; Eukaryota. DR HOGENOM; CLU_012847_2_0_1; -. DR InParanoid; Q8TFH7; -. DR OMA; YSHPYWK; -. DR PhylomeDB; Q8TFH7; -. DR PRO; PR:Q8TFH7; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005737; C:cytoplasm; HDA:PomBase. DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:PomBase. DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000213; F:tRNA-intron endonuclease activity; IBA:GO_Central. DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central. DR CDD; cd22363; tRNA-intron_lyase_C; 1. DR Gene3D; 3.40.1350.10; -; 1. DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf. DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf. DR InterPro; IPR006677; tRNA_intron_Endonuc_cat-like. DR InterPro; IPR006676; tRNA_splic. DR InterPro; IPR016589; tRNA_splic_SEN2. DR PANTHER; PTHR21227; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 1. DR PANTHER; PTHR21227:SF0; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 1. DR Pfam; PF01974; tRNA_int_endo; 1. DR PIRSF; PIRSF011789; tRNA_splic_SEN2; 1. DR SUPFAM; SSF53032; tRNA-intron endonuclease catalytic domain-like; 1. PE 3: Inferred from homology; KW Lyase; Reference proteome; tRNA processing. FT CHAIN 1..380 FT /note="Probable tRNA-splicing endonuclease subunit sen2" FT /id="PRO_0000109461" FT ACT_SITE 281 FT /evidence="ECO:0000250" FT ACT_SITE 289 FT /evidence="ECO:0000250" FT ACT_SITE 325 FT /evidence="ECO:0000250" SQ SEQUENCE 380 AA; 44608 MW; E458D08F0D920249 CRC64; MSKNHEVYKD ALPISLAYPL PPIILTNPLT WIPYIYRYLF RKTPRQVQWQ CQLHESDLSC VVTDSEAIKK FWTSGFFGKG NLSRSEPTWH TRTKRSLGLL GFDEDLVAEE VTARRRFQRK QFKAQRAYRE NRARERQLLL ENGKPIPASL EEDAELPEYL TKSLKDFSRV SENPYHITSV PNVEHLQLTF PEAFFLASLG VLRINYENPN FELLPILKLF ANIVANSVAL THDYSLQQSH EDPIIEPDNK FLTELAAYFY FRQQGWVVKN GTKFSVDFLL YKKGPVFSHA EFAILLIPCV GNKQKYNMQW HEVHCLNRVI AQVKKSLILC YVQCPSIEDF NKIWKNQASM NEWDWAESVL RQYLIRCVTL RRWVPSRNRD //