ID   RLGM2_TRYBB             Reviewed;         416 AA.
AC   P86924; P82864; Q4GYS0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=RNA-editing ligase 2, mitochondrial;
DE            Short=RNA ligase 2;
DE            EC=6.5.1.3 {ECO:0000250|UniProtKB:P86927};
DE   AltName: Full=TbMP48;
DE   Flags: Precursor;
GN   Name=REL2; Synonyms=KREL2, MP48;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-37; 58-72;
RP   118-139; 143-151; 200-207; 217-224; 255-263; 302-323; 336-340; 371-384 AND
RP   410-416, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=Treu 427;
RX   PubMed=11134327; DOI=10.1128/mcb.21.2.380-389.2001;
RA   Panigrahi A.K., Gygi S.P., Ernst N.L., Igo R.P. Jr., Palazzo S.S.,
RA   Schnaufer A., Weston D.S., Carmean N., Salavati R., Aebersold R.,
RA   Stuart K.D.;
RT   "Association of two novel proteins TbMP52 and TbMP48 with the Trypanosoma
RT   brucei RNA editing complex.";
RL   Mol. Cell. Biol. 21:380-389(2001).
CC   -!- FUNCTION: RNA editing in kinetoplastid mitochondria inserts and deletes
CC       uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
CC       {ECO:0000269|PubMed:11134327}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.;
CC         EC=6.5.1.3; Evidence={ECO:0000250|UniProtKB:P86927};
CC   -!- SUBUNIT: Component of the RNA editing complex, a 1600 kDa complex
CC       composed of at least 20 proteins. {ECO:0000269|PubMed:11134327}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11134327}.
CC   -!- SIMILARITY: Belongs to the RNA ligase 2 family. {ECO:0000305}.
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DR   EMBL; AY009111; AAG27063.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86924; -.
DR   SMR; P86924; -.
DR   GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR   GO; GO:0031019; C:mitochondrial mRNA editing complex; IDA:GeneDB.
DR   GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR   GO; GO:0045293; C:mRNA editing complex; IDA:GeneDB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003972; F:RNA ligase (ATP) activity; TAS:GeneDB.
DR   GO; GO:0016556; P:mRNA modification; TAS:GeneDB.
DR   Gene3D; 1.10.10.1810; -; 1.
DR   InterPro; IPR012647; RNA_lig_RNL2.
DR   InterPro; IPR021122; RNA_ligase_dom_REL/Rnl2.
DR   InterPro; IPR041948; Rnl1/2_C_sf.
DR   InterPro; IPR040609; Rnl2_C.
DR   Pfam; PF09414; RNA_ligase; 1.
DR   Pfam; PF18043; T4_Rnl2_C; 1.
DR   TIGRFAMs; TIGR02307; RNA_lig_RNL2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Mitochondrion;
KW   Nucleotide-binding; RNA-binding; Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:11134327"
FT   CHAIN           18..416
FT                   /note="RNA-editing ligase 2, mitochondrial"
FT                   /id="PRO_0000411985"
FT   ACT_SITE        57
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         56..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         269..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  47477 MW;  A6E338CD64549147 CRC64;
     MLRRLGVRHF RRTPLLFVGG DGSIFERYTE IDNSNERRIN ALKGCGMFED EWIATEKVHG
     ANFGIYSIEG EKMIRYAKRS GIMPPNEHFF GYHILIPELQ RYVTSIREML CEKQKKKLHV
     VLINGELFGG KYDHPSVPKT RKTVMVAGKP RTISAVQTDS FPQYSPDLHF YAFDIKYKET
     EGGDYTTLVY DEAIELFQRV PGLLYARAVI RGPMSKVAAF DVERFVTTIP PLVGMGNYPL
     TGNWAEGLVV KHSRLGMAGF DPKGPTVLKF KCTAFQEIST DRAQGPRVDE MRNVRRDSIN
     RAGVQLPDLE SIVQDPIQLE ASKLLLNHVC ENRLKNVLSK IGTEPFEKEE MTPDQLATLL
     AKDALKDFLK DTEPSIVNIP VLIRKDLTRY VIFESRRLVC SQWKDILKRQ SPDFSE