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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
 
 
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