SEN54_YEAST
ID SEN54_YEAST Reviewed; 467 AA.
AC Q02825; D6W3T4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=tRNA-splicing endonuclease subunit SEN54;
DE AltName: Full=Splicing endonuclease of 54 kDa;
DE AltName: Full=tRNA-intron endonuclease SEN54;
GN Name=SEN54; OrderedLocusNames=YPL083C; ORFNames=LPF3C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 322-332, 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).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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: 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. May be required to embody the molecular ruler of the
CC complex.
CC -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC SEN2, SEN15, SEN34 and SEN54. Interacts directly with SEN2.
CC {ECO:0000269|PubMed:9200603}.
CC -!- INTERACTION:
CC Q02825; P16658: SEN2; NbExp=4; IntAct=EBI-16829, EBI-16953;
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. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Present with 531 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEN54 family. {ECO:0000305}.
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DR EMBL; U41849; AAB68256.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11350.1; -; Genomic_DNA.
DR PIR; S61105; S61105.
DR RefSeq; NP_015242.1; NM_001183897.1.
DR AlphaFoldDB; Q02825; -.
DR BioGRID; 36098; 111.
DR ComplexPortal; CPX-1832; tRNA-intron endonuclease complex.
DR DIP; DIP-4452N; -.
DR IntAct; Q02825; 5.
DR MINT; Q02825; -.
DR STRING; 4932.YPL083C; -.
DR MaxQB; Q02825; -.
DR PaxDb; Q02825; -.
DR PRIDE; Q02825; -.
DR EnsemblFungi; YPL083C_mRNA; YPL083C; YPL083C.
DR GeneID; 856022; -.
DR KEGG; sce:YPL083C; -.
DR SGD; S000006004; SEN54.
DR VEuPathDB; FungiDB:YPL083C; -.
DR eggNOG; KOG4772; Eukaryota.
DR GeneTree; ENSGT00390000004214; -.
DR HOGENOM; CLU_028449_0_1_1; -.
DR InParanoid; Q02825; -.
DR OMA; FNVWKPQ; -.
DR BioCyc; MetaCyc:G3O-33989-MON; -.
DR BioCyc; YEAST:G3O-33989-MON; -.
DR BRENDA; 4.6.1.16; 984.
DR PRO; PR:Q02825; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02825; protein.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IDA:SGD.
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 InterPro; IPR024337; tRNA_splic_suSen54.
DR InterPro; IPR024336; tRNA_splic_suSen54_N.
DR PANTHER; PTHR21027; PTHR21027; 1.
DR Pfam; PF12928; tRNA_int_end_N2; 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..467
FT /note="tRNA-splicing endonuclease subunit SEN54"
FT /id="PRO_0000194034"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 54649 MW; 363A703856DE724E CRC64;
MQFAGKKTDQ VTTSNPGFEE EEEEEEELQQ DWSQLASLVS KNAALSLPKR GEKDYEPDGT
NLQDLLLYNA SKAMFDTISD SIRGTTVKSE VRGYYVPHKH QAVLLKPKGS FMQTMGRADS
TGELWLDFHE FVYLAERGTI LPYYRLEAGS NKSSKHETEI LLSMEDLYSL FSSQQEMDQY
FVFAHLKRLG FILKPSNQEA AVKTSFFPLK KQRSNLQAIT WRLLSLFKIQ ELSLFSGFFY
SKWNFFFRKY TTSPQLYQGL NRLVRSVAVP KNKKELLDAQ SDREFQKVKD IPLTFKVWKP
HSNFKKRDPG LPDFQVFVYN KNDDLQHFPT YKELRSMFSS LDYKFEFLSE IEDDDDWETN
SYVEDIPRKE YIHKRSAKSQ TEKSESSMKA SFQKKTAQSS TKKKRKAYPP HIQQNRRLKT
GYRSFIIAIM DNGLISFVKM SEADFGSESV WYTPNTQKKV DQRWKKH
