TUTT_DROME
ID TUTT_DROME Reviewed; 560 AA.
AC Q9VI58;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Terminal uridylyltransferase Tailor {ECO:0000305};
DE Short=TUTase Tailor {ECO:0000305};
DE EC=2.7.7.52 {ECO:0000269|PubMed:26145174, ECO:0000269|PubMed:26145176};
GN Name=Tailor {ECO:0000312|FlyBase:FBgn0037470};
GN ORFNames=CG1091 {ECO:0000312|FlyBase:FBgn0037470};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL48740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48740.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48740.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-280.
RX PubMed=26145176; DOI=10.1016/j.molcel.2015.05.033;
RA Reimao-Pinto M.M., Ignatova V., Burkard T.R., Hung J.H.,
RA Manzenreither R.A., Sowemimo I., Herzog V.A., Reichholf B.,
RA Farina-Lopez S., Ameres S.L.;
RT "Uridylation of RNA hairpins by Tailor confines the emergence of microRNAs
RT in Drosophila.";
RL Mol. Cell 59:203-216(2015).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DISRUPTION PHENOTYPE.
RX PubMed=26145174; DOI=10.1016/j.molcel.2015.05.034;
RA Bortolamiol-Becet D., Hu F., Jee D., Wen J., Okamura K., Lin C.J.,
RA Ameres S.L., Lai E.C.;
RT "Selective suppression of the splicing-mediated microRNA pathway by the
RT terminal uridyltransferase Tailor.";
RL Mol. Cell 59:217-228(2015).
CC -!- FUNCTION: Uridylyltransferase which mediates terminal uridylation of
CC miRNAs, leading to their degradation. Has high specificity for
CC splicing-derived miRNAs (mirtrons) and other miRNA substrates
CC containing a 3'-G terminal nucleotide. Appears to be a major suppressor
CC of mirtron biogenesis. {ECO:0000269|PubMed:26145174,
CC ECO:0000269|PubMed:26145176}.
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:0000269|PubMed:26145174, ECO:0000269|PubMed:26145176};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:26145174, ECO:0000269|PubMed:26145176};
CC Note=No activity with Mn(2+) or Ca(2+). {ECO:0000269|PubMed:26145174};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26145176}.
CC -!- DISRUPTION PHENOTYPE: Viable. Fertility is significantly reduced.
CC {ECO:0000269|PubMed:26145174, ECO:0000269|PubMed:26145176}.
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DR EMBL; AE014297; AAF54068.3; -; Genomic_DNA.
DR EMBL; AY071118; AAL48740.1; -; mRNA.
DR RefSeq; NP_649693.3; NM_141436.3.
DR PDB; 5Z4A; X-ray; 1.64 A; A=202-550.
DR PDB; 5Z4C; X-ray; 1.65 A; A=202-560.
DR PDB; 5Z4D; X-ray; 1.80 A; A=202-560.
DR PDB; 5Z4J; X-ray; 1.82 A; A=202-560.
DR PDB; 5Z4M; X-ray; 1.74 A; A=202-560.
DR PDB; 6I0S; X-ray; 1.90 A; A=180-560.
DR PDB; 6I0T; X-ray; 2.00 A; A=180-560.
DR PDB; 6I0U; X-ray; 2.00 A; A=180-560.
DR PDB; 6I0V; X-ray; 1.85 A; A=180-560.
DR PDBsum; 5Z4A; -.
DR PDBsum; 5Z4C; -.
DR PDBsum; 5Z4D; -.
DR PDBsum; 5Z4J; -.
DR PDBsum; 5Z4M; -.
DR PDBsum; 6I0S; -.
DR PDBsum; 6I0T; -.
DR PDBsum; 6I0U; -.
DR PDBsum; 6I0V; -.
DR AlphaFoldDB; Q9VI58; -.
DR SMR; Q9VI58; -.
DR IntAct; Q9VI58; 3.
DR STRING; 7227.FBpp0305518; -.
DR PRIDE; Q9VI58; -.
DR DNASU; 40847; -.
DR EnsemblMetazoa; FBtr0081640; FBpp0081154; FBgn0037470.
DR GeneID; 40847; -.
DR KEGG; dme:Dmel_CG1091; -.
DR UCSC; CG1091-RB; d. melanogaster.
DR CTD; 40847; -.
DR FlyBase; FBgn0037470; Tailor.
DR VEuPathDB; VectorBase:FBgn0037470; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156640; -.
DR InParanoid; Q9VI58; -.
DR PhylomeDB; Q9VI58; -.
DR BRENDA; 2.7.7.52; 1994.
DR SignaLink; Q9VI58; -.
DR BioGRID-ORCS; 40847; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Tailor; fly.
DR GenomeRNAi; 40847; -.
DR PRO; PR:Q9VI58; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037470; Expressed in eye disc (Drosophila) and 42 other tissues.
DR ExpressionAtlas; Q9VI58; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:FlyBase.
DR GO; GO:0031124; P:mRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; IDA:FlyBase.
DR GO; GO:0031054; P:pre-miRNA processing; IMP:FlyBase.
DR GO; GO:0071076; P:RNA 3' uridylation; IMP:FlyBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-mediated gene silencing; Transferase.
FT CHAIN 1..560
FT /note="Terminal uridylyltransferase Tailor"
FT /id="PRO_0000436845"
FT DOMAIN 455..522
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT REGION 169..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O13833"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:26145176"
FT MUTAGEN 280
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26145176"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:6I0V"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6I0V"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:5Z4A"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 365..380
FT /evidence="ECO:0007829|PDB:5Z4A"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 448..464
FT /evidence="ECO:0007829|PDB:5Z4A"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:5Z4D"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:5Z4A"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 492..500
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:5Z4A"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:5Z4A"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:5Z4A"
FT HELIX 530..546
FT /evidence="ECO:0007829|PDB:5Z4A"
SQ SEQUENCE 560 AA; 63945 MW; 31DF346DA4C8529D CRC64;
MRIEPGDSFW TKKAMFSNAE RQYFETVRPR KTSLPGSTAP NIAAPVTKAT KKNKTMAEMM
PNKLLYMNPL TMEAHFFLQT LNSVNQTTNP PQLDPHLANL LERIMVGIES YLDRNPTYVL
PQEMAAPGEG VAFVQPQELQ TIKRTFSCSS CSNRIVGTTI AKAVAHLSEQ HPKPNPNNQP
VQPHPTHQTK QEKKQAQVKA RQHITVRLPK KARAMIVGEI TNVFKDKYPI ADKLKVIPEY
DVIEQDLCKL LSPGFPKQPL RVYKFGSRIT GIGNRSSDLD LFVDIGNTFH TFEHRASNAT
VAKLRAMRKF FCDSEDWRLI NFIEQARVPI IKTCHLPTGI ECDICLNSMG FCNTNLLKYI
FESQPLTQYM CIYVKNWLER CKLTEQISTY SITLMVIYFL QLQALLPPIA MLQIEDAANQ
AVLVGPWVVN FAQKSFSELG LQQLKATVPV IKGFLRNFFA YFAKFDYEHF LVCPYIGQAN
VEIAKIERML HARYSAYVSD NPECSIQLKK PMVVQDPIQL NHNVTKAVTK YGLQTFVDYC
QQTAELLEEP STNWRQRYAF
