MPSS3_TRYBB
ID MPSS3_TRYBB Reviewed; 1136 AA.
AC A0A120KVW2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=Mitochondrial 3' processome subunit 3 {ECO:0000303|PubMed:26833087};
DE Flags: Precursor;
GN Name=MPSS3 {ECO:0000303|PubMed:26833087};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1] {ECO:0000312|EMBL:AME15292.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION IN THE MPSOME
RP COMPLEX, INTERACTION WITH KRET1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
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: As part of the mitochondrial 3' processome (MPsome), involved
CC in the maturation of guided RNA (gRNA) precursors.
CC {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 (PubMed:26833087).
CC {ECO:0000269|PubMed:26833087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26833087}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the procyclic stage (at protein
CC level). {ECO:0000269|PubMed:26833087}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the procyclic stage
CC causes moderate growth defect without affecting the production of
CC guided RNAs (gRNA). {ECO:0000269|PubMed:26833087}.
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DR EMBL; KT282122; AME15292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120KVW2; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Mitochondrion; Transit peptide.
FT TRANSIT 1..97
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 98..1136
FT /note="Mitochondrial 3' processome subunit 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450684"
SQ SEQUENCE 1136 AA; 125672 MW; 6A1BF54301E1EE85 CRC64;
MKKAWAQLER VLQPSSSRVN RALITQQLEA LYALPINCEA ACRWEDAQRL FLRCNGHRPY
YAGIMDQSTD NRLAVASFEE NMLALQQRGL VCTTVGDKAP PCVVGGQTSR GLCRRSSIVC
VNVGSCADLD LNMHEDCDET LLTLLHGVVV PYLHFRIVYG TGVSPPLVPR APGPAICGAS
HDLSLQNELH MDSCVALLHP RGLCSSNCNN KAYRTAATLV RGAVSLATSD TLLHQRQDGC
FTLHPDAMKL GSPRLFALQL WWNKEVGPVI QRGVEQSVKT DEVLSGAWIE VARKRVEELV
ERGGDDLPQP LRNMTRDDVA AFAADATLCW TLSAFDCNYK RLGPAQPACR LQFSEEARLS
MALELMQTVK ASLVKQPTGI PISELSATVC WPAASAWIGE KSLTEALTQF PAHFNVVNVE
GKLVVMHGHL TGPSDNVTAE EVSEWLAAGH SEGLQKPCVA ASPSDLTFHR ETDLVVRAVA
FLRKRHFGNV PVTYGELCGA LLPKNNGKND GDSDTLLNVL LRYDVLAADT AKGDSSINIQ
CGLRDGDAIR LSVREDRALR ALEAFRTTSR SAFQLYTEAI EPFLTCCRGA MRENGSCVVP
LTLLERWLQV ERLSLQSKEL LDILRSAEGP YRIDEELCNV VLTNHTAKGE VLTPAFSLPA
TPPPPPPPAV SSRLTFEAQI SRVLKTQRPD RLLHFVQTIL HAVFDLILPH VSAPSGVPVR
MLMRRIRWGS FVVTLGSLTS FVEAFDGLFF EVLSNASSHG EEKRDDVDLI VSAYKGPVSP
WLLYARLIVR LFPADVDIPL GLIAEALSWS SRFAPMFGDL PSLLRRVGRQ CRNGQLLAKV
EMVRPVCDQD DACLWELLAK IRREAHLHHL ERSSGETGQY VLLSETELYA YLPNDVKGER
WNSTVKEEGA RCLATMAVHR LPHFFEWHVD NTDTTTRYVR VVLPFSTPPT GVVCFVEEYV
CPLLRQHKQT TIAELDEQLG WSHGAFDAHP AGSQAAGGTP SATSLCGLLR RYVESMHSPK
IILEPQETTL SPLHHHVHVM PNSAVYTSPE DMLLLLNGLR ISNEGITRVL PTHKPVSLFE
LISQQLDLHQ PFREGLTTLE RGSRWNVMLA CESDSMDDCL QELDNCTGDI LVWCEG