RLGM1_TRYBB
ID RLGM1_TRYBB Reviewed; 469 AA.
AC P86926; P82863; Q38FA5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=RNA-editing ligase 1, mitochondrial;
DE Short=RNA ligase 1;
DE EC=6.5.1.3 {ECO:0000250|UniProtKB:P86927};
DE Flags: Precursor;
GN Name=REL1;
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 45-68; 88-107;
RP 137-143; 154-172; 195-245; 300-307; 373-379; 402-409 AND 444-469, FUNCTION,
RP 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).
RN [2]
RP IDENTIFICATION IN THE RECC COMPLEX, INTERACTION WITH MEAT1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19465686; DOI=10.1261/rna.1538809;
RA Aphasizheva I., Ringpis G.E., Weng J., Gershon P.D., Lathrop R.H.,
RA Aphasizhev R.;
RT "Novel TUTase associates with an editosome-like complex in mitochondria of
RT Trypanosoma brucei.";
RL RNA 15:1322-1337(2009).
CC -!- FUNCTION: Essential for RNA editing. RNA editing in kinetoplastid
CC mitochondria inserts and deletes uridylates at multiple sites in pre-
CC mRNAs as directed by guide RNAs. {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 (editosome), a 1600 kDa
CC complex composed of at least 20 proteins (PubMed:11134327,
CC PubMed:19465686). Interacts with terminal uridylyltransferase MEAT1
CC (PubMed:19465686). {ECO:0000269|PubMed:11134327,
CC ECO:0000269|PubMed:19465686}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11134327,
CC ECO:0000269|PubMed:19465686}.
CC -!- SIMILARITY: Belongs to the RNA ligase 2 family. {ECO:0000305}.
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DR EMBL; AY009110; AAG27062.1; -; Genomic_DNA.
DR AlphaFoldDB; P86926; -.
DR SMR; P86926; -.
DR BindingDB; P86926; -.
DR ChEMBL; CHEMBL4105928; -.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR GO; GO:0031019; C:mitochondrial 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; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009451; P:RNA modification; IDA: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 Pfam; PF09414; RNA_ligase; 1.
DR TIGRFAMs; TIGR02307; RNA_lig_RNL2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Mitochondrion;
KW mRNA processing; Nucleotide-binding; RNA-binding; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11134327"
FT CHAIN 45..469
FT /note="RNA-editing ligase 1, mitochondrial"
FT /id="PRO_0000411984"
FT REGION 450..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P86927"
FT BINDING 59..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P86927"
FT BINDING 86..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P86927"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P86927"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P86927"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P86927"
FT BINDING 307..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P86927"
SQ SEQUENCE 469 AA; 52296 MW; DF7C4A266A0B0F55 CRC64;
MQLQRLGAPL LKRLVGGCIR QSTAPIMPCV VVSGSGVFLT PVRTYMPLPN DQSDFSPYIE
IDLPSESRIQ SLHKSGLAAQ EWVACEKVHG TNFGIYLINQ GDHEVVRFAK RSGIMDPNEN
FFGYHILIDE FTAQIRILND LLKQKYGLSR VGRLVLNGEL FGAKYKHPLV PKSEKWCTLP
NGKKFPIAGV QIQREPFPQY SPELHFFAFD IKYSVSGAEE DFVLLGYDEF VEFSSKVPNL
LYARALVRGT LDECLAFDVE NFMTPLPALL GLGNYPLEGN LAEGVVIRHV RRGDPAVEKH
NVSTIIKLRC SSFMELKHPG KQKELKETFI DTVRSGALRR VRGNVTVISD SMLPQVEAAA
NDLLLNNVSD GRLSNVLSKI GREPLLSGEV SQVDVVLMLA KDALKDFLKE VDSLVLNTTL
AFRKLLITNV YFESKRLVEQ KWKELMQEEA AAQSEAIPPL SPAAPTKGE
