ID E9AY21_LEIMU Unreviewed; 510 AA.
AC E9AY21;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN ORFNames=LMXM_26_0390 {ECO:0000313|EMBL:CBZ27862.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ27862.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000256|ARBA:ARBA00024498};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; FR799579; CBZ27862.1; -; Genomic_DNA.
DR RefSeq; XP_003876343.1; XM_003876294.1.
DR AlphaFoldDB; E9AY21; -.
DR SMR; E9AY21; -.
DR GeneID; 13449264; -.
DR KEGG; lmi:LMXM_26_0390; -.
DR VEuPathDB; TriTrypDB:LmxM.26.0390; -.
DR OMA; WVERTTY; -.
DR OrthoDB; 1080369at2759; -.
DR PhylomeDB; E9AY21; -.
DR Proteomes; UP000007259; Chromosome 26.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:UniProt.
DR GO; GO:0071076; P:RNA 3' uridylation; IEA:UniProt.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.50; -; 1.
DR Gene3D; 3.30.70.1970; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR041060; Ret2_MD.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF50; RNA EDITING 3' TERMINAL URIDYLYL TRANSFERASE 2; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF18528; Ret2_MD; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBZ27862.1}.
FT DOMAIN 88..148
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 188..280
FT /note="RNA editing 3' terminal uridylyl transferase 2
FT middle"
FT /evidence="ECO:0000259|Pfam:PF18528"
FT DOMAIN 387..447
FT /note="PAP-associated"
FT /evidence="ECO:0000259|Pfam:PF03828"
SQ SEQUENCE 510 AA; 57702 MW; B068869007927A52 CRC64;
MYAPTPLRLY VAVTRGLCSS AVAASSSTDA ASSPNVASSS ASEGVSYASH LVASKDHYAQ
WGRVLLEENR KRIGPEQMFR TAIRAQQQLQ MLADKWTPDA KIYCCGSLVT HGQMEWGSDL
DLACVFDDPY PDHSVQAKRT EKLWSVVKRY VPQFLRSNLL ALTEARTPVV KLRYVNDDKV
ARGRYAVLTE EEDRKSRTTL WDIRNRHLDS KDLEYIATKM GRENIEGIWV ERTTYGCRCA
VQCTSREQAI EAVGFFPDGV IMTKGMREDY TRDMLDLRYV PEMFMYKWDI SFVAYGVKNS
YLLRHYLHSG PPAARHAAMA AKAWGKASGV GLGTAAMLTS YAVTVMFVHY LLATRQLAWI
DPWSLAHPVH MPRFPDFSPL LDCDPVELGK LLHGFFTYYA AHFNYEKNII SLSRPRLSLR
SDVNWNFPQS KQGTFSYLLG IEDPYEDVGI GGLNLGRHLH AAKFNQVKQE FARAAATMER
YVPSNAPEKT ILGARRGGTS NHHHHHNRFD
//