ID   P90629_9TRYP            Unreviewed;       206 AA.
AC   P90629;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   08-OCT-2025, entry version 107.
DE   SubName: Full=GBP21 {ECO:0000313|EMBL:AAC47460.1};
GN   Name=gBP21 {ECO:0000313|EMBL:AAC47460.1};
OS   Trypanosoma brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5691 {ECO:0000313|EMBL:AAC47460.1};
RN   [1] {ECO:0000313|EMBL:AAC47460.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IsTaR 1.7 {ECO:0000313|EMBL:AAC47460.1};
RA   Koeller J., Goeringer H.U.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAC47460.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IsTaR 1.7 {ECO:0000313|EMBL:AAC47460.1};
RX   PubMed=9013632; DOI=10.1074/jbc.272.6.3749;
RA   Koller J., Muller U.F., Schmid B., Missel A., Kruft V., Stuart K.,
RA   Goringer H.U.;
RT   "Trypanosoma brucei gBP21. An arginine-rich mitochondrial protein that
RT   binds to guide RNA with high affinity.";
RL   J. Biol. Chem. 272:3749-3757(1997).
RN   [3] {ECO:0007829|PDB:2GIA, ECO:0007829|PDB:2GID}
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 20-206.
RX   PubMed=16923390; DOI=10.1016/j.cell.2006.06.047;
RA   Schumacher M.A., Karamooz E., Zikova A., Trantirek L., Lukes J.;
RT   "Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal
RT   RNA matchmaking mechanism.";
RL   Cell 126:701-711(2006).
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DR   EMBL; U61382; AAC47460.1; -; Genomic_DNA.
DR   PDB; 2GIA; X-ray; 1.89 A; B/D=20-206.
DR   PDB; 2GID; X-ray; 3.35 A; B/D/J/K=20-206.
DR   PDB; 2GJE; X-ray; 3.37 A; D=20-206.
DR   AlphaFoldDB; P90629; -.
DR   SMR; P90629; -.
DR   IntAct; P90629; 1.
DR   VEuPathDB; TriTrypDB:Tb1125.11.1710; -.
DR   VEuPathDB; TriTrypDB:Tb427_110021800; -.
DR   VEuPathDB; TriTrypDB:Tb927.11.1710; -.
DR   VEuPathDB; TriTrypDB:Tbg972.11.1830; -.
DR   HOGENOM; CLU_1334278_0_0_1; -.
DR   EvolutionaryTrace; P90629; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR   GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR   GO; GO:0003723; F:RNA binding; IDA:GeneDB.
DR   GO; GO:0016556; P:mRNA modification; IMP:GeneDB.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:GeneDB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   FunFam; 2.30.31.40:FF:000001; Mitochondrial RNA binding protein 1; 1.
DR   Gene3D; 2.30.31.40; -; 1.
DR   InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR   InterPro; IPR032680; SUN1_N.
DR   Pfam; PF09387; MRP; 1.
DR   SUPFAM; SSF54447; ssDNA-binding transcriptional regulator domain; 1.
DR   PDBsum; 2GIA; -.
DR   PDBsum; 2GID; -.
DR   PDBsum; 2GJE; -.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2GIA, ECO:0007829|PDB:2GID}.
FT   DOMAIN          9..167
FT                   /note="SUN"
FT                   /evidence="ECO:0000259|Pfam:PF09387"
FT   REGION          179..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  23253 MW;  BE2EB3B9AFC9228F CRC64;
     MIRLACLRGP AMRSAWSRGA STFSGVQSLP KFEIHDVRDD PALGTMTRVA VDGKLLLISQ
     YPQLGPRKVD PNDLSPQFDA DRRISVRLRH VDLAYLVGVC KERVPRHRME TKAYTLDFEK
     SAQGYHLHGK VHRVASQRME DWSVKFDNHF AVTLEHFLES ALDESFGFRQ HYATRAAEGG
     EKIAATSSAE GGARRKRSVS DTSRYH
//