ID   A0A286YDD7_MOUSE        Unreviewed;      1089 AA.
AC   A0A286YDD7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-SEP-2023, entry version 32.
DE   RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE            EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE   Flags: Fragment;
GN   Name=Tut7 {ECO:0000313|Ensembl:ENSMUSP00000153376.2,
GN   ECO:0000313|MGI:MGI:2387179};
GN   Synonyms=Zcchc6 {ECO:0000313|MGI:MGI:2387179};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000153376.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000153376.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000153376.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000153376.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000153376.2};
RG   Ensembl;
RL   Submitted (MAY-2023) to UniProtKB.
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}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000256|ARBA:ARBA00008593}.
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DR   AlphaFoldDB; A0A286YDD7; -.
DR   SMR; A0A286YDD7; -.
DR   jPOST; A0A286YDD7; -.
DR   ProteomicsDB; 361683; -.
DR   Antibodypedia; 13297; 58 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000224480.2; ENSMUSP00000153376.2; ENSMUSG00000035248.10.
DR   AGR; MGI:2387179; -.
DR   MGI; MGI:2387179; Tut7.
DR   VEuPathDB; HostDB:ENSMUSG00000035248; -.
DR   GeneTree; ENSGT00940000156859; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000035248; Expressed in basioccipital bone and 295 other tissues.
DR   ExpressionAtlas; A0A286YDD7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010467; P:gene expression; IEA:UniProt.
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; -; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR045100; TUTase_dom.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF34; TERMINAL URIDYLYLTRANSFERASE 7; 1.
DR   Pfam; PF03828; PAP_assoc; 2.
DR   Pfam; PF19088; TUTase; 1.
DR   Pfam; PF16631; TUTF7_u4; 1.
DR   Pfam; PF00098; zf-CCHC; 3.
DR   SMART; SM00343; ZnF_C2HC; 3.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 3.
DR   PROSITE; PS50158; ZF_CCHC; 3.
PE   1: Evidence at protein level;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Proteomics identification {ECO:0007829|EPD:A0A286YDD7,
KW   ECO:0007829|MaxQB:A0A286YDD7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          559..574
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          941..955
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          1046..1062
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          338..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..460
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000153376.2"
SQ   SEQUENCE   1089 AA;  122923 MW;  85D250A6BA31037C CRC64;
     SGLLCKVSAG NENAWLTTKH LTALGKLEPR LVPLVIAFRY WAKLCSIDRP EEGGLPPYVF
     ALMAVFFLQQ RKEPLLPVYL GSWIEEFSLN KLGNFSLKDV EKDSVVWEYT DNSTGDTSSA
     KEEAPKETAA KKGQVPLTFN IKHQPSVPVG QLWVELLRFY ALEFNLADLV ISIRVKELIS
     RESKDWPKKR IAIEDPYSVK RNVARTLNNQ PVFEYILHCL RTTYKYFALP HKVTKPNLTK
     PPSPVTCVSD PYREAKNGGP EPQATNIDKL GNAAVAQDPG VQTSGDCRAQ LVTLKNTTEE
     VGSPAKEKTG GVHIPAHQES SGCVQAEVSC EGLEDATAEL PETGSDNEEV RRKTKHPLST
     DDQGLSSSKH PELQNCGSLC GLQADNTLEL VAEECNSCAS LDNKAEVNEE RIEGAEELEE
     AAALSCFSPS VQSRTSAAMH FDDEEEEEEE EEEEEPRLSI NLTEDEEGVA NEHQVDSRYA
     GSGEEDALSE EDDLAEPAKG EDTGECGENV GGTLLIDLNR ITLKEESFPE EDLPGDQSEF
     FYEFRKLTFT KGKSPTVVCS LCKREGHLKK DCPEDFKRVQ LEPLPPLTPK FSNILDQVCV
     QCYKDFSPTI VEDQAREHIR QNLESFIKQD FPGTKLSLFG SSKNGFGFKQ SDLDVCMTIN
     GHETAEGLDC VRTIEELARV LRKHSGLRNI LPITTAKVPI VKFFHLRSGL EVDISLYNTL
     ALHNTRLLSA YSAIDPRVKY LCYTMKVFTK MCDIGDASRG SLSSYAYTLM VLYFLQQRSP
     PVIPVLQEIY KGEKKPEILV DGWNIYFFDQ INELPTCWPE YGKNTEPVGQ LWLGLLRFYT
     EEFDFKEHVI SIRRKSLLTT FKKQWTSKYI VIEDPFDLNH NLGAGLSRKM TNFIMKAFIN
     GRRVFGIPVK GFPKDNPSKL AYFFDPDVLT EGELAPNDRC CRICGKIGHF MKDCPMRRKV
     RRRRDQEDTP NQRYSESKEK RSKEDKEIQN KYTEKEVSTK EDKLTPCAAA KAKPVRAAVD
     LGREKLLRTP TEKWKRQDDR DSREKRCFIC GREGHIKKEC PQFKGSPGSL SSKYMTQGRA
     SVKRTQQES
//