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SEN34_SCHPO
ID   SEN34_SCHPO             Reviewed;         284 AA.
AC   O60156;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable tRNA-splicing endonuclease subunit sen34;
DE            EC=4.6.1.16;
DE   AltName: Full=tRNA-intron endonuclease sen34;
GN   Name=sen34; ORFNames=SPBC19C7.07c;
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. It probably carries the active
CC       site for 3'-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 sen15 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA19575.1; -; Genomic_DNA.
DR   PIR; T39813; T39813.
DR   RefSeq; NP_596163.1; NM_001022083.2.
DR   AlphaFoldDB; O60156; -.
DR   BioGRID; 277117; 1.
DR   STRING; 4896.SPBC19C7.07c.1; -.
DR   MaxQB; O60156; -.
DR   PaxDb; O60156; -.
DR   EnsemblFungi; SPBC19C7.07c.1; SPBC19C7.07c.1:pep; SPBC19C7.07c.
DR   GeneID; 2540591; -.
DR   KEGG; spo:SPBC19C7.07c; -.
DR   PomBase; SPBC19C7.07c; sen34.
DR   VEuPathDB; FungiDB:SPBC19C7.07c; -.
DR   eggNOG; KOG4133; Eukaryota.
DR   HOGENOM; CLU_049366_0_0_1; -.
DR   InParanoid; O60156; -.
DR   OMA; FIAYPGD; -.
DR   PhylomeDB; O60156; -.
DR   PRO; PR:O60156; -.
DR   Proteomes; UP000002485; Chromosome II.
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; IPR016690; tRNA_splic_SEN34.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   PIRSF; PIRSF017250; tRNA_splic_SEN34; 1.
DR   SUPFAM; SSF53032; SSF53032; 1.
DR   TIGRFAMs; TIGR00324; endA; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..284
FT                   /note="Probable tRNA-splicing endonuclease subunit sen34"
FT                   /id="PRO_0000109467"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  32808 MW;  F40AFEBE0C50F567 CRC64;
     MEDEKFPISY VHGKFLVFDV QAVEVFRKNY HILGTLVGTL PQLPQQNVFL GLPMELSKEE
     AFYLIEKGIS YIVDDTKVHK QLLENTTKDD VKQCLKKRQS LAYDQMIAAK KKENEKKIEI
     MKKLGRTLPL DPLNYDEHDS FDLSWIPVDT VTTRIAEKSS MNDDFHKEED VFENLDINRY
     LMFKSLVDTG FYLNPGLRFG CQFVAYPGDA LRYHSHYLVN SYKWDQEIPV LFLIGGGRLG
     TAVKKTWLIG GSNDRNINMN GEKSKEELLL LPVRHFSIEW AGFG
 
 
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