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Database: UniProt
Entry: A0A0A1U510_ENTIV
LinkDB: A0A0A1U510_ENTIV
Original site: A0A0A1U510_ENTIV 
ID   A0A0A1U510_ENTIV        Unreviewed;       344 AA.
AC   A0A0A1U510;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE            EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN   ORFNames=EIN_487910 {ECO:0000313|EMBL:ELP89279.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP89279.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP89279.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP89279.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KB206670; ELP89279.1; -; Genomic_DNA.
DR   RefSeq; XP_004256050.1; XM_004256002.1.
DR   AlphaFoldDB; A0A0A1U510; -.
DR   EnsemblProtists; ELP89279; ELP89279; EIN_487910.
DR   GeneID; 14888235; -.
DR   KEGG; eiv:EIN_487910; -.
DR   VEuPathDB; AmoebaDB:EIN_487910; -.
DR   OrthoDB; 21395at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:RHEA.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProt.
DR   GO; GO:0061157; P:mRNA destabilization; IEA:UniProt.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR045862; Trf4-like.
DR   InterPro; IPR045100; TUTase_dom.
DR   PANTHER; PTHR23092:SF15; INACTIVE NON-CANONICAL POLY(A) RNA POLYMERASE PROTEIN TRF4-2-RELATED; 1.
DR   PANTHER; PTHR23092; POLY(A) RNA POLYMERASE; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF19088; TUTase; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   4: Predicted;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ELP89279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW   Transferase {ECO:0000313|EMBL:ELP89279.1}.
FT   DOMAIN          22..122
FT                   /note="TUTase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF19088"
FT   DOMAIN          199..252
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          312..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38908 MW;  1E67E97A447DF564 CRC64;
     MWLRSVCPTD KLTLTEEIKL FTRYISLTPN EQELRQISYQ KVSQLLTNRY PGCEVTIYGS
     YVSGFSLPSS DIDLVLSFSE EVSKNQVKKL LFKISTICRS SKFLRVEDVI TNAKVPIIKL
     LDLDTTISID LSINCEGGID SSALTHSLLT SSQFTQEIAL FVKYLVFQNN LNEPYHGGIG
     SYAIVLLTAT FLKFYPQHSL GRALVEFLNF YGNIFKMGKT GVSYQHGFFS LVEKNLFEED
     SLVIEDPCDE GNNVGRSSFK FNAVQFLFKK TLMGINLIIK NPEGMYLPSG SRLAKVVAIP
     KSLQKYREAI DAVKSEQKSE EKTEEKEEVE VMKSPEIYNE PLVQ
//
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