RLGM1_TRYB2
ID RLGM1_TRYB2 Reviewed; 469 AA.
AC P86927; P82863; Q38FA5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=RNA-editing ligase 1, mitochondrial;
DE Short=RNA ligase 1;
DE EC=6.5.1.3 {ECO:0000269|PubMed:11251122, ECO:0000269|PubMed:15465048};
DE AltName: Full=TbMP52;
DE Flags: Precursor;
GN Name=REL1; Synonyms=MP52; ORFNames=Tb09.160.2970;
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=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).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11251122; DOI=10.1126/science.1058955;
RA Schnaufer A., Panigrahi A.K., Panicucci B., Igo R.P. Jr., Wirtz E.,
RA Salavati R., Stuart K.;
RT "An RNA ligase essential for RNA editing and survival of the bloodstream
RT form of Trypanosoma brucei.";
RL Science 291:2159-2162(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 51-324 IN COMPLEX WITH ATP,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15465048; DOI=10.1016/j.jmb.2004.08.041;
RA Deng J., Schnaufer A., Salavati R., Stuart K.D., Hol W.G.J.;
RT "High resolution crystal structure of a key editosome enzyme from
RT Trypanosoma brucei: RNA editing ligase 1.";
RL J. Mol. Biol. 343:601-613(2004).
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:11251122,
CC ECO:0000269|PubMed:15465048}.
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:0000269|PubMed:11251122,
CC ECO:0000269|PubMed:15465048};
CC -!- SUBUNIT: Component of the RNA editing complex (editosome), a 1600 kDa
CC complex composed of at least 20 proteins (By similarity). Interacts
CC with terminal uridylyltransferase MEAT1 (By similarity).
CC {ECO:0000250|UniProtKB:P86926}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P86926}.
CC -!- SIMILARITY: Belongs to the RNA ligase 2 family. {ECO:0000305}.
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DR EMBL; CM000207; EAN76515.1; -; Genomic_DNA.
DR RefSeq; XP_803740.1; XM_798647.1.
DR PDB; 1XDN; X-ray; 1.20 A; A=51-324.
DR PDBsum; 1XDN; -.
DR AlphaFoldDB; P86927; -.
DR SMR; P86927; -.
DR PaxDb; P86927; -.
DR GeneID; 3660066; -.
DR KEGG; tbr:Tb09.160.2970; -.
DR VEuPathDB; TriTrypDB:Tb927.9.4360; -.
DR eggNOG; ENOG502QV9S; Eukaryota.
DR InParanoid; P86927; -.
DR OMA; NQEWVAC; -.
DR BRENDA; 6.5.1.3; 6519.
DR EvolutionaryTrace; P86927; -.
DR Proteomes; UP000008524; Chromosome 9.
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:0005739; C:mitochondrion; IDA:UniProtKB.
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; IEA:UniProtKB-EC.
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 3D-structure; ATP-binding; Ligase; Mitochondrion; mRNA processing;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT CHAIN 45..469
FT /note="RNA-editing ligase 1, mitochondrial"
FT /id="PRO_0000278161"
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:0000305|PubMed:15465048"
FT BINDING 59..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT BINDING 86..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT BINDING 307..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15465048,
FT ECO:0007744|PDB:1XDN"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 128..146
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 152..164
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 201..216
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1XDN"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:1XDN"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1XDN"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:1XDN"
SQ SEQUENCE 469 AA; 52226 MW; 8864BD07D98C335F CRC64;
MQLQRLGAPL LKRLVGGCIR QSTAPIMPCV VVSGSGGFLT 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 SQVDVALMLA KDALKDFLKE VDSLVLNTTL
AFRKLLITNV YFESKRLVEQ KWKELMQEEA AAQSEAIPPL SPAAPTKGE
