SEN34_YEAST
ID SEN34_YEAST Reviewed; 275 AA.
AC P39707; D6VPM0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=tRNA-splicing endonuclease subunit SEN34;
DE EC=4.6.1.16;
DE AltName: Full=Splicing endonuclease of 34 kDa;
DE AltName: Full=tRNA-intron endonuclease SEN34;
GN Name=SEN34; OrderedLocusNames=YAR008W; ORFNames=FUN4;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION, PROTEIN SEQUENCE OF 206-223, SUBUNIT, AND MUTAGENESIS OF
RP HIS-217.
RX PubMed=9200603; DOI=10.1016/s0092-8674(00)80270-6;
RA Trotta C.R., Miao F., Arn E.A., Stevens S.W., Ho C.K., Rauhut R.,
RA Abelson J.N.;
RT "The yeast tRNA splicing endonuclease: a tetrameric enzyme with two active
RT site subunits homologous to the archaeal tRNA endonucleases.";
RL Cell 89:849-858(1997).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12925762; DOI=10.1091/mbc.e02-11-0757;
RA Yoshihisa T., Yunoki-Esaki K., Ohshima C., Tanaka N., Endo T.;
RT "Possibility of cytoplasmic pre-tRNA splicing: the yeast tRNA splicing
RT endonuclease mainly localizes on the mitochondria.";
RL Mol. Biol. Cell 14:3266-3279(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
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.
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. {ECO:0000269|PubMed:9200603}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12925762}.
CC Endomembrane system {ECO:0000269|PubMed:12925762}; Peripheral membrane
CC protein {ECO:0000269|PubMed:12925762}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12925762,
CC ECO:0000269|PubMed:16823961}; Cytoplasmic side
CC {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}. Note=The
CC tRNA splicing endonuclease complex is predominantly associated with the
CC outer membrane of mitochondria, suggesting that tRNA splicing mainly
CC takes place on the mitochondrial surface.
CC -!- MISCELLANEOUS: The tRNA splicing endonuclease complex is present with
CC 100 molecules/cell.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC {ECO:0000305}.
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DR EMBL; L22015; AAC04961.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06990.1; -; Genomic_DNA.
DR PIR; S40903; S40903.
DR RefSeq; NP_009405.1; NM_001178212.1.
DR AlphaFoldDB; P39707; -.
DR SMR; P39707; -.
DR BioGRID; 31794; 13.
DR ComplexPortal; CPX-1832; tRNA-intron endonuclease complex.
DR DIP; DIP-3794N; -.
DR IntAct; P39707; 4.
DR STRING; 4932.YAR008W; -.
DR MaxQB; P39707; -.
DR PaxDb; P39707; -.
DR PRIDE; P39707; -.
DR EnsemblFungi; YAR008W_mRNA; YAR008W; YAR008W.
DR GeneID; 851267; -.
DR KEGG; sce:YAR008W; -.
DR SGD; S000000066; SEN34.
DR VEuPathDB; FungiDB:YAR008W; -.
DR eggNOG; KOG4133; Eukaryota.
DR GeneTree; ENSGT00390000003912; -.
DR HOGENOM; CLU_049366_0_0_1; -.
DR InParanoid; P39707; -.
DR OMA; FIAYPGD; -.
DR BioCyc; MetaCyc:G3O-28870-MON; -.
DR BioCyc; YEAST:G3O-28870-MON; -.
DR BRENDA; 4.6.1.16; 984.
DR PRO; PR:P39707; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39707; protein.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IDA:SGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..275
FT /note="tRNA-splicing endonuclease subunit SEN34"
FT /id="PRO_0000109468"
FT ACT_SITE 209
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT ACT_SITE 250
FT /evidence="ECO:0000250"
FT MUTAGEN 217
FT /note="H->A: Loss of function; induces a marked
FT accumulation of 5' exon and intron-3' exon 2/3 molecule."
FT /evidence="ECO:0000269|PubMed:9200603"
SQ SEQUENCE 275 AA; 31313 MW; CCEA2A30209AB03F CRC64;
MPPLVFDIDH IKLLRKWGIC GVLSGTLPTA AQQNVFLSVP LRLMLEDVLW LHLNNLADVK
LIRQEGDEIM EGITLERGAK LSKIVNDRLN KSFEYQRKFK KDEHIAKLKK IGRINDKTTA
EELQRLDKSS NNDQLIESSL FIDIANTSMI LRDIRSDSDS LSRDDISDLL FKQYRQAGKM
QTYFLYKALR DQGYVLSPGG RFGGKFIAYP GDPLRFHSHL TIQDAIDYHN EPIDLISMIS
GARLGTTVKK LWVIGGVAEE TKETHFFSIE WAGFG
