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   03-AUG-2022, entry version 105.
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   BioGRID; 280474; 1.
DR   STRING; 4896.SPAPB17E12.07c.1; -.
DR   MaxQB; Q8TFH7; -.
DR   PaxDb; Q8TFH7; -.
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; LPAFYPN; -.
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; ISO:PomBase.
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; ISO:PomBase.
DR   GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; ISO:PomBase.
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; PTHR21227; 1.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   PIRSF; PIRSF011789; tRNA_splic_SEN2; 1.
DR   SUPFAM; SSF53032; SSF53032; 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