MPSS1_TRYBB
ID MPSS1_TRYBB Reviewed; 1728 AA.
AC A0A120KVR8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Mitochondrial 3' processome subunit 1 {ECO:0000303|PubMed:26833087};
DE Flags: Precursor;
GN Name=MPSS1 {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:AME15290.1}
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 and reduces production of guided RNAs
CC (gRNA) due to a block in the processing of gRNA precursors.
CC {ECO:0000269|PubMed:26833087}.
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DR EMBL; KT282120; AME15290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120KVR8; -.
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..117
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 118..1728
FT /note="Mitochondrial 3' processome subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450682"
FT REGION 45..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1728 AA; 191362 MW; AC4C87253A3B507A CRC64;
MRRLILSQTL RVAGRHRPPV AMFLQRFYRG HGISTALPLH YSKRHRKREG RMYGKPLRPV
SDGENGASGD GGVLTRWEAV VSSRHQCESP VQTLAKSEKP KKAENTVAGK MTGSSRFSHR
RDHSAYPSGV QPAPLATSGL PTQSSERQQQ KQIGQQQVPL DALHRLFKVH AVMRTNYEAL
GKCTKVLKSF STACAEALLQ LGVLQKEQPS AMERKGFIDV QLCKSRVTEA SKNGTSSPCF
VLPPESPLYR TTIKFPTITV EHVLTTTVPA GCGAKDSGGD IMSVDMEGAA PFPMGHCESR
PSTSAGNGVT VEYDCEGDVL SHGAAWNSII EGFGQLALNL KQNASVSDFA QLAETLAYFK
WVKDEEQVGW GTEDCVVKKF REAMANAKDT SASGSDPNTS DVSAALAAIA ESFLRKIPRV
DCIGSAVVHR GGERTAPSVH AIDVMLNLAL RMCLSQWHAM SHFERMNIVL FCTYPWFAED
LSIAAGLCLT QSYLQSLLRA DADVTYQHTF HYVRRVSRLC WPCIHDTDSA PVKKLLFPRD
PQGTAVSSHA LEAVSVEEKD NQLNQKEGLQ GEEQATTTSE SKLMWLPSFK DASCVSYGSS
MKQRAAYELL LLWMTCVNPS GLHRSSPHGR YVSATGIAII DVDLFVTQRF RTGKSKDEWL
LLHPVEGDVV ASVTIRTMVQ HCETPYALTR LFFCNFHSVL PHIWGGIGAR RREIIWTAWC
RAVAQPLVNT LSGSDEGQRE DDGGMQTLQI TVDNADRTLD YLKPLISALT SDELFLRLIM
RCADKSLEEM ACEIGSGNNT LPLSKWCAQL AGFVYSVAFA LHCRAKREGC NRDGGPSRPN
TATDSANKKV VSGKQTDNLP KGTQEDISDL QLQFKAAVSA LLRKLSAGDT QVAEQLLHHF
YEPHFSGDQE REVVEDIQRH LQQVCDSQSR DALHAWIECS ARASCEATVP LKEELLCKWQ
RTVLEADAGL PVVLPTIVEC CRGLVGLVKK RGRNISGRRQ GQQRGTESTT VGEESSCKEV
FSKEELPVVI TVLSRAMLTR TSTVSTVGLT KISSEISTLL SSCGYETADG NTSGGGRNGR
ELCDTNTATI TSATAGERTV ELELILSGEI DQKAGELPWI TILEAVQLQL VPYTVVKNLL
TSFKGGCDNG KERLRWQELQ RDFQRKRHHR LVGNTLVFRW YGCAVPNDEG WEDGSGLMRP
MAEDRDNVHS ASHQGRTSTE LGAFTRRLLK TLARAEVTRL DDRKEITTQT FVVGPSDDSA
TRHPTPGQEE DANLQRLDLL FRVHTLAAHI LMTASTKKPH MIHELYDTLL HLVERVMPTT
PNAPGNASDL LLLWLVGSAV AVGLRFRPNF LIKWPSTPEV SSGNLKSCPS AEEKTVHILR
DIEPYLQSEL LRPTVRLRFV INVLVALRSL ELLGARIDVE GLHMDQLLVR ASADRRLLSR
HVNLFLIGCS ALQSTQSSIL HTALHLREAK YNLSFAEIER AFVAIALSAD TFARQHEALM
EQNYQQQQNR TLSVTVAANN TTPALRVSPV QLRHAWSALG RRVLENAGES PTDLFVRGLQ
CAAAVGCIDS ALYQQLLSYV VEFRWEDLHI LDWVMILRTV RQSFENRRNL EAYLKEPLQA
FMLTMTDSGD NSTEQSVQKV NLKNHEGEQL LEGLCLFAEA LPGLFIGDRE LWGLLWQALG
SQWSACFNAA SNIEEQQRIT AWLQEINASY AWAARAAGFR GLDEPTAL