DSS1_TRYBB
ID DSS1_TRYBB Reviewed; 743 AA.
AC Q86MA2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Mitochondrial exoribonuclease DSS-1 {ECO:0000303|PubMed:15470249};
DE Short=TbDSS-1 {ECO:0000303|PubMed:15470249};
DE EC=3.1.13.1 {ECO:0000269|PubMed:26833087};
DE AltName: Full=3'-5' exonuclease DSS1 {ECO:0000303|PubMed:26833087};
DE Flags: Precursor;
GN Name=DSS1 {ECO:0000303|PubMed:15470249};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1] {ECO:0000312|EMBL:AAO74636.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15470249; DOI=10.1128/ec.3.5.1206-1216.2004;
RA Penschow J.L., Sleve D.A., Ryan C.M., Read L.K.;
RT "TbDSS-1, an essential Trypanosoma brucei exoribonuclease homolog that has
RT pleiotropic effects on mitochondrial RNA metabolism.";
RL Eukaryot. Cell 3:1206-1216(2004).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18032430; DOI=10.1093/nar/gkm690;
RA Mattiacio J.L., Read L.K.;
RT "Roles for TbDSS-1 in RNA surveillance and decay of maturation by-products
RT from the 12S rRNA locus.";
RL Nucleic Acids Res. 36:319-329(2008).
RN [3] {ECO:0000305}
RP IDENTIFICATION IN THE MITOCHONDRIAL DEGRADOSOME COMPLEX, INTERACTION WITH
RP SUV3, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19540236; DOI=10.1016/j.febslet.2009.06.024;
RA Mattiacio J.L., Read L.K.;
RT "Evidence for a degradosome-like complex in the mitochondria of Trypanosoma
RT brucei.";
RL FEBS Lett. 583:2333-2338(2009).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MPSOME COMPLEX,
RP INTERACTION WITH KRET1 AND MPSS2, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-202.
RX PubMed=26833087; DOI=10.1016/j.molcel.2016.01.004;
RA Suematsu T., Zhang L., Aphasizheva I., Monti S., Huang L., Wang Q.,
RA Costello C.E., Aphasizhev R.;
RT "Antisense Transcripts Delimit Exonucleolytic Activity of the Mitochondrial
RT 3' Processome to Generate Guide RNAs.";
RL Mol. Cell 61:364-378(2016).
CC -!- FUNCTION: 3'-5'exoribonuclease which is involved in the post-
CC transcriptional processing, editing and degradation of mitochondrial
CC RNAs, including mRNAs, rRNAs and guided RNAs (gRNA) (PubMed:15470249,
CC PubMed:26833087). As part of the mitochondrial 3' processome (MPsome),
CC involved in the maturation of guided RNA (gRNA) precursors by
CC catalyzing the processive 3'-5' degradation of uridylated gRNA
CC precursors (PubMed:26833087). Plays a role in the degradation of 12S
CC rRNA processing intermediates and maturation by-products
CC (PubMed:18032430). {ECO:0000269|PubMed:15470249,
CC ECO:0000269|PubMed:18032430, ECO:0000269|PubMed:26833087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000269|PubMed:26833087};
CC -!- SUBUNIT: Component of the mitochondrial 3' processome (MPsome) complex
CC composed at least of terminal uridylyltransferase KRET1/TUT1, 3'-5'
CC exonuclease DSS1, MPSS1, MPSS2 and MPSS3 (PubMed:26833087). Within the
CC complex, interacts with KRET1 and MPSS2 (PubMed:26833087). Component of
CC the mitochondrial degradosome complex composed at least of 3'-5'
CC exonuclease DSS1 and helicase SUV3 (PubMed:19540236). Within the
CC complex, interacts with helicase SUV3 (PubMed:19540236).
CC {ECO:0000269|PubMed:19540236, ECO:0000269|PubMed:26833087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15470249,
CC ECO:0000269|PubMed:19540236, ECO:0000269|PubMed:26833087}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the procyclic stage (at protein
CC level). {ECO:0000269|PubMed:15470249, ECO:0000269|PubMed:19540236,
CC ECO:0000269|PubMed:26833087}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the procyclic stage
CC causes moderate growth defect and reduces the levels of several
CC mitochondrial RNAs, including never edited, unedited, and edited mRNAs
CC as well as guided RNAs (gRNA) (PubMed:15470249, PubMed:26833087). Also
CC results in the accumulation of fragments of the flanking region
CC upstream of the mature 5'end of 12S rRNA, the 5' flanking sequence and
CC the truncated 12S rRNA sequence, and the 5' full-length 12S rRNAs
CC (PubMed:18032430). {ECO:0000269|PubMed:15470249,
CC ECO:0000269|PubMed:18032430, ECO:0000269|PubMed:26833087}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; AY233297; AAO74636.1; -; mRNA.
DR AlphaFoldDB; Q86MA2; -.
DR SMR; Q86MA2; -.
DR GO; GO:0045025; C:mitochondrial degradosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:UniProtKB.
DR GO; GO:0004532; F:exoribonuclease activity; IMP:GeneDB.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IMP:UniProtKB.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IMP:GeneDB.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; IMP:GeneDB.
DR GO; GO:0000963; P:mitochondrial RNA processing; IDA:UniProtKB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Exonuclease; Hydrolase; Mitochondrion; Nuclease; Transit peptide.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 68..743
FT /note="Mitochondrial exoribonuclease DSS-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450685"
FT REGION 320..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 202
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26833087"
SQ SEQUENCE 743 AA; 83357 MW; 6D0FAD12C3A9EDB2 CRC64;
MTPRRVAKLV QFSGSYLNTE WARKFILGSL LQRYNPQSLT TVGSSAAGNS GEDASLDKEL
LHLQRSLSEV WSLPAQPLDA VSEGRILRLL ARYATGEGVM SIEALNELSH VLSCIRGSPQ
RVEGPIDMEE LLLAIGYAKP GDNLRRVAFA GELQYPPSAL AHMRAHLRDD MERDGSDPFD
ILRVVTHNPA YAIDSASTSE VDDAIGVHKD PVTGEECFVV YVSDATVYCP FDSPLEQLTA
RLLTTTTYLP EGVFFMLPKP IVDAATLRED RPCRTFDIRF QIDEVTGELK NYSVGVGWLH
KLRRITYDEV QALYDEEAQV GNQHHHTERE STQASPAKRE EGKKGMVASG GTSSCRPSWM
TVEDESILRR IYRAAQKRYE TRQLRAGDRF IHADLPEPLI KVGAGAQVLS VEDQIIGTRD
ARLAVAEMMI AANEVCSRVA QENHLSIPFR GTRELSLDHV AAKSYREPHG VVSVQSLDPQ
YVFFAEAMQR SIRQLSGVTR AVYFHTPIYH AGLDTHNYTH STSPLRRYAD MLVHHQLKVW
LWRTSHCSSG GGVLHSAQKS SPVLIEQPIA EHTMATLCSM ISSKQEQSSI LQESSQRYWL
LKHIKQNILT KSPHHRFICL VGDTRSVKCA PEYARFVVEC SHDSPSQPDG GVHRTVPWAG
RWKQRHHEYL YVSDIYITEL QFAHVVLHSL PDVVVGAVVE CEVREVHPTQ GYLSLAIVKV
WSGGDERRFE PLWKKCLLPS LDS
