MPSS2_TRYBB
ID MPSS2_TRYBB Reviewed; 1642 AA.
AC A0A120KVR5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Mitochondrial 3' processome subunit 2 {ECO:0000303|PubMed:26833087};
DE Flags: Precursor;
GN Name=MPSS2 {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:AME15291.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION IN THE MPSOME
RP COMPLEX, INTERACTION WITH DSS1, 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 DSS1 (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; KT282121; AME15291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120KVR5; -.
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..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..1642
FT /note="Mitochondrial 3' processome subunit 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450683"
FT REGION 43..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1642 AA; 181585 MW; 84B20A7BEF57FAD3 CRC64;
MGLPFLCHTR VCLFSNKIPF VLCGSRFAPA TLHAHHTAAG GGETLNFPEL SSPSTSKEPS
VGSDSPQKKN KKQAFDALAR WCGGHQQLLM RIQQSAEDTS AGVVFETPLT EVDSAAIRWL
QGSTEQLTCG QSLLVCSFVC EVLYCQLNSA SGGIGVEEAQ RLQIHALTNR IAALLQRADE
SNKLESQPLS VLMSCAYVVQ RLKYVDNPLF GETQRSLVKV PPSIMFALLH KLRGDGLGKL
FQLDERTATD VCLSFLFIAT EEHRQAFFSS GDAALVSNVL RRLVRYTASK TRRMRIQKEG
DIIDLLTVDS PSDGGARQTP VCTSGTGFTS PSMRECAMIM QNVSFSSPSN RLELLLYLLC
VRRNLAQCSL KDIELVPTVL STVANIRSAE ACSIRKKIIS QLWLPENNPT LVAQLLVHSG
ESIPRYVTYL QGVPASKLSP RDAAQVILCA GTYLSYESLQ LYIMAALRDI MPSSSLVTLG
AETTSASVPA TASVPTRVPA CDSLETVLSV LLMRVEEKGG SLSEVEKDAC MEYIRRLNEL
IDWCASAPTS SPKPALQRLT LLTKLFNRGL VVHAPETVVE LAVQSLQLDP GNTMMNTLKC
VSEALPLVSD DKKRSIIIEK MISYSGTRTT SSVIRFLLLL APLVDADSPH SCELVEQLLK
FHTLNPHKLR QASVEGVAKG IDVYTLLLIN GIDFLLASGD WRSSPSQLQN VITTWVRDYT
LYVMDPARKQ KIDDGAAAHV APATKGEKTD VVQHQQPSRL NEGGELPTLS GPNDEELEQV
FTCLLRAGVK LPHAFSSELL SRIRRLQAKR NPADGTDQQV VFPLPAHFVF CCKLDVPVEV
SVTPEMMKYH IDACDYRIIH CVITAFFSAA GTFKHNINDL LLCNMRLASR SFELFIQRLG
EEASRSFRPA TVSSVVANTL RFVVNHITKQ ERCQRVLRKL NEKGGIEAGE EELEGDRSLI
AEHTRLGELL TRMIAYLSGA HVKNVGLSVL DRLSLLSPAC GEYLMMRLST QLSEFTQVEL
LYLVQKYPKS QDLVAELLGK SDLVSSMDFG DYMRVMRNLP MPINALVIGA HLPGLNFQWC
TRILSSLSVR HESVPLHLLA SVLRRLNDVT ESATLTDRNI AFVVLQKYLQ FDQTSGDGGD
LEERQRLIKC SCDKLLVLSR INSLDTLKEF LVEFPEALSG VICESLSKHV VQHIVGGLLK
DLDGLLTLCR LLHRHKLLTS DVKVAIVDGF FMKTLQSEVE GRANIEGESS QGLQPLNSVR
GASLKTTHPV SNVLALALLL SDGPLHFPGA SNSSSTICGD NERCAVSSMF QVVKESYTSP
RDRLLIANTL VGQKGPNALT VVAKEICTEL IENCESVTSN DFSRLLQCIS RLKCWSELDL
ANSRFDEVFQ RSCTQADAHS RCVAFRAVSF EADIFRRYES FMIPLLQETV DVMSNEDLET
VLSSVLSLPF TEALESLIDA IGTRLLRMID QCRRSALIRL LQCHAAFGIQ DDALVSVCVA
TLTDQCGRDF RLDTAQVLAL LQAAVDLDFF LPPKLVTSCF TWLEHHVENM TITQLGHAVR
LAVDVEVGYT AAVHTLTLRA LEQRDAIRSN ASFREAVEML CDEFSAEIPW HLRAPVLRRR
YQSERLLEYL DKRRLAVDST VA