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Database: UniProt
Entry: R0G027_9BRAS
LinkDB: R0G027_9BRAS
Original site: R0G027_9BRAS 
ID   R0G027_9BRAS            Unreviewed;       764 AA.
AC   R0G027;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE            EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
GN   ORFNames=CARUB_v10024989mg {ECO:0000313|EMBL:EOA28757.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA28757.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KB870808; EOA28757.1; -; Genomic_DNA.
DR   RefSeq; XP_006295859.1; XM_006295797.1.
DR   AlphaFoldDB; R0G027; -.
DR   STRING; 81985.R0G027; -.
DR   GeneID; 17888111; -.
DR   KEGG; crb:17888111; -.
DR   eggNOG; KOG2277; Eukaryota.
DR   OrthoDB; 170176at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
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; IPR045100; TUTase_dom.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF40; POLY(A) RNA POLYMERASE GLD2; 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   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          448..548
FT                   /note="TUTase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF19088"
FT   DOMAIN          656..714
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  85898 MW;  2238415C97301620 CRC64;
     MADGGAASPA PPSENVGDFI LSLLQQNTRP SPSQQGGPPQ HLDPAIAAVG PTVNPFPPSI
     WQSSNGRDHR PGTLNPSWPH AAFSPPPNLS PNLLGFPQFT PNPFPLNQFD GNQRLSPEDA
     YRLGFPATGT HAIQSMVQQQ QPPPPPQSDY RKLVFGSFSG DATQSLNGLR NGNLKYDSIH
     QEQLMRNPQS VVLNSNPEDP NLSHHRNHDL HEQRGGHNGR GGNWGPIGNN VRGFKSTPTP
     PPPGFSSNQR GWDMNLGSKD DDRGIGSFQR NHDRAMWEHS NLNAEADRLR GLSLQNESKF
     NLSQQIDHPG PPKGTSLHSV STADAANSFS MLNKEARGGS ERKDELGQLS KMKREGNEKS
     GPGDDEIDDF GEDIVDSLLL EVDTDDKDAK DGKKNSKTSR EKESRVDNRG RWLLSQRLRE
     RKMYMACRND IHRYDAPFMA VYKSLIPAEE ELEKQRQLMA QLENLVAKEW PHAKLYLYGS
     CANSFGFPKS DIDVCLAIED DDINKSDMLL KLADILESDN LQNVQALTRA RVPIVKLMDP
     VTGISCDICI NNVLAVVNTK LLRDYARIDV RLRQLAFIVK HWAKSRKVNE TYQGTLSSYA
     YVLMCIHFLQ LRRPPILPCL QEMKPTYSVR VDNIRCSYFD DVGRLDNFGS SNRETIAELV
     WGFFNYWAYA HDYANTVVSV RTGSILGKRE KDWTRRVGND RHLICIEDPF ETSHDLGRVV
     DKFSIRVLRE EFERAAEIMH QDRNPCAKLF EPYLPEDNNG QGHK
//
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