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SEN15_YEAST
ID   SEN15_YEAST             Reviewed;         128 AA.
AC   Q04675; D6VZN3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=tRNA-splicing endonuclease subunit SEN15;
DE   AltName: Full=Splicing endonuclease of 15 kDa;
DE   AltName: Full=tRNA-intron endonuclease SEN15;
GN   Name=SEN15; OrderedLocusNames=YMR059W; ORFNames=YM9796.12;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
RP   CHARACTERIZATION, PROTEIN SEQUENCE OF 1-11, AND SUBUNIT.
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   [4]
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).
CC   -!- FUNCTION: Non-catalytic subunit of the tRNA-splicing endonuclease
CC       complex, a complex responsible for identification and cleavage of the
CC       splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice
CC       sites to release the intron. The products are an intron and two tRNA
CC       half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There
CC       are no conserved sequences at the splice sites, but the intron is
CC       invariably located at the same site in the gene, placing the splice
CC       sites an invariant distance from the constant structural features of
CC       the tRNA body.
CC   -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC       SEN2, SEN15, SEN34 and SEN54. Interacts directly with SEN34.
CC       {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}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12925762}; Cytoplasmic side
CC       {ECO:0000269|PubMed:12925762}. Note=The tRNA splicing endonuclease
CC       complex is predominantly associated with the outer membrane of
CC       mitochondria, suggesting that tRNA splicing mainly takes place on the
CC       mitochondrial surface.
CC   -!- MISCELLANEOUS: The tRNA splicing endonuclease complex is present with
CC       100 molecules/cell.
CC   -!- SIMILARITY: Belongs to the SEN15 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA89769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z49703; CAA89769.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006946; DAA09957.1; -; Genomic_DNA.
DR   RefSeq; NP_013775.2; NM_001182557.1.
DR   AlphaFoldDB; Q04675; -.
DR   SMR; Q04675; -.
DR   BioGRID; 35234; 88.
DR   ComplexPortal; CPX-1832; tRNA-intron endonuclease complex.
DR   DIP; DIP-5802N; -.
DR   IntAct; Q04675; 81.
DR   STRING; 4932.YMR059W; -.
DR   MaxQB; Q04675; -.
DR   PaxDb; Q04675; -.
DR   PRIDE; Q04675; -.
DR   TopDownProteomics; Q04675; -.
DR   EnsemblFungi; YMR059W_mRNA; YMR059W; YMR059W.
DR   GeneID; 855081; -.
DR   KEGG; sce:YMR059W; -.
DR   SGD; S000004663; SEN15.
DR   VEuPathDB; FungiDB:YMR059W; -.
DR   eggNOG; ENOG502SC4F; Eukaryota.
DR   HOGENOM; CLU_083361_2_0_1; -.
DR   InParanoid; Q04675; -.
DR   OMA; VYYFVYK; -.
DR   BioCyc; MetaCyc:G3O-32762-MON; -.
DR   BioCyc; YEAST:G3O-32762-MON; -.
DR   BRENDA; 4.6.1.16; 984.
DR   PRO; PR:Q04675; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04675; protein.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IC:ComplexPortal.
DR   GO; GO:0000214; C:tRNA-intron endonuclease complex; IDA:SGD.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR   GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IDA:SGD.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   InterPro; IPR042777; Sen15_fungi.
DR   InterPro; IPR018593; tRNA-endonuc_su_Sen15.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR   PANTHER; PTHR28518; PTHR28518; 1.
DR   Pfam; PF09631; Sen15; 1.
DR   SUPFAM; SSF53032; SSF53032; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..128
FT                   /note="tRNA-splicing endonuclease subunit SEN15"
FT                   /id="PRO_0000194028"
SQ   SEQUENCE   128 AA;  14890 MW;  17DF8B5F3824DF82 CRC64;
     MATTDIISLV KNNLLYFQMW TEVEILQDDL SWKGNSLRLL RGRPPHKLSN DVDTEHENSL
     SSPRPLEFIL PINMSQYKEN FLTLECLSQT FTHLCSPSTE RILLAIINDD GTIVYYFVYK
     GVRKPKRN
 
 
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