RLGM2_TRYB2
ID RLGM2_TRYB2 Reviewed; 416 AA.
AC P86925; P82864; Q4GYS0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
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; ORFNames=Tb927.1.3030;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=12907729; DOI=10.1093/nar/gkg674;
RA Hall N., Berriman M., Lennard N.J., Harris B.R., Hertz-Fowler C.,
RA Bart-Delabesse E.N., Gerrard C.S., Atkin R.J., Barron A.J., Bowman S.,
RA Bray-Allen S.P., Bringaud F., Clark L.N., Corton C.H., Cronin A.,
RA Davies R., Doggett J., Fraser A., Grueter E., Hall S., Harper A.D.,
RA Kay M.P., Leech V., Mayes R., Price C., Quail M.A., Rabbinowitsch E.,
RA Reitter C., Rutherford K., Sasse J., Sharp S., Shownkeen R., MacLeod A.,
RA Taylor S., Tweedie A., Turner C.M., Tait A., Gull K., Barrell B.,
RA Melville S.E.;
RT "The DNA sequence of chromosome I of an African trypanosome: gene content,
RT chromosome organisation, recombination and polymorphism.";
RL Nucleic Acids Res. 31:4864-4873(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1;
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
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:0000250|UniProtKB:P86924}.
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA ligase 2 family. {ECO:0000305}.
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DR EMBL; AL929603; CAJ16514.1; -; Genomic_DNA.
DR RefSeq; XP_001219001.1; XM_001219000.1.
DR AlphaFoldDB; P86925; -.
DR SMR; P86925; -.
DR STRING; 5691.CAJ16514; -.
DR PaxDb; P86925; -.
DR PRIDE; P86925; -.
DR GeneID; 4357372; -.
DR KEGG; tbr:TB927.1.3030; -.
DR VEuPathDB; TriTrypDB:Tb927.1.3030; -.
DR eggNOG; ENOG502RW2V; Eukaryota.
DR InParanoid; P86925; -.
DR OMA; CTAFQEI; -.
DR Proteomes; UP000008524; Chromosome 1.
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 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT CHAIN 18..416
FT /note="RNA-editing ligase 2, mitochondrial"
FT /id="PRO_0000022473"
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; 47577 MW; 9D06C2289EAE5E48 CRC64;
MLRRLGVRHF RRTPLLFVGG DGSIFERYTE IDNSNERRIN ALKGCGMFED EWIATEKVHG
ANFGIYSIEG EKMIRYAKRS GIMPPNEHFF GYHILIPELQ RYITSIREML CEKQKKKLHV
VLINGELFGG KYDHPSVPKT RKTVMVAGKP RTISAVQTDS FPQYSPDLHF YAFDIKYKET
EDGDYTTLVY DEAIELFQRV PGLLYARAVI RGPMSKVAAF DVERFVTTIP PLVGMGNYPL
TGNWAEGLVV KHSRLGMAGF DPKGPTVLKF KCTAFQEIST DRAQGPRVDE MRNVRRDSIN
RAGVQLPDLE SIVQDPIQLE ASKLLLNHVC ENRLKNVLSK IGTEPFEKEE MTPDQLATLL
AKDVLKDFLK DTEPSIVNIP VLIRKDLTRY VIFESRRLVC SQWKDILKRQ SPDFSE
