ID   TUT1_BOVIN              Reviewed;         871 AA.
AC   Q1JPD6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=U6 snRNA-specific terminal uridylyltransferase 1;
DE            Short=U6-TUTase;
DE            EC=2.7.7.52;
DE   AltName: Full=RNA-binding motif protein 21;
DE            Short=RNA-binding protein 21;
GN   Name=TUT1; Synonyms=RBM21;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Highly specific terminal uridylyltransferase that
CC       exclusively accepts U6 snRNA as substrate. U6 snRNA is unique in
CC       that nucleotides are both added to and removed from its 3'-end.
CC       U6-TUTase is responsible for a controlled elongation reaction that
CC       results in the restoration of the four 3'-terminal UMP-residues
CC       found in newly transcribed U6 snRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; BT025417; ABF57373.1; -; mRNA.
DR   IPI; IPI00705794; -.
DR   RefSeq; NP_001073791.1; -.
DR   UniGene; Bt.21690; -.
DR   Ensembl; ENSBTAG00000011846; Bos taurus.
DR   GeneID; 616339; -.
DR   KEGG; bta:616339; -.
DR   HOVERGEN; Q1JPD6; -.
DR   BRENDA; 2.7.7.52; 251.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR012677; a_b_plait_nuc_bd.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR000504; RRM_RNP1.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein; RNA-binding;
KW   Transferase.
FT   CHAIN         1    871       U6 snRNA-specific terminal
FT                                uridylyltransferase 1.
FT                                /FTId=PRO_0000254185.
FT   DOMAIN       56    128       RRM.
FT   MOD_RES     748    748       Phosphoserine (By similarity).
SQ   SEQUENCE   871 AA;  93811 MW;  E681018AFBA18459 CRC64;
     MAAVDSDIEP LPRGGFRCCL CHITTANQPS LDAHLGGRKH RHLVELRATR KAQGLRSVFV
     SGFPRDVDST QLSEYFQAFG PVASVVMDKD KGVFAIVEMG DLGAREAVLS QPQHSLGGRR
     LRVRPREQIE FQSPASRSPK RVAPDSHQLI KALAEAPDVE AQMVKLVGLR ELSEAERQLR
     SLVVALMQEV FAEFFPGCVV HPFGSSINSF DVHGCDLDLF LDLGDLDEPQ PAPKAPESPS
     LDSALASPLD PQALACTPAS PPDSQPPASP QDSEALDFEA PSSSLAPRTP DSALASETLA
     SPRSLPPASP LQEDQGDGDQ GKAVELAEAL KGEKAEGGAM LELVGSILRG CVPGVYRVQT
     VPSARCPVVK FCHRPSGLHG DISLSNRLAL HNSRFLSLCS ELDGRVRPLV YTLRCWAQGR
     GLSGSGPLLN NYALTLLVIY FLQTRDPPVL PTVSQLTQKA GEQVEVDGWD CSFPRDASRL
     EPSTNKEPLS SLLAQFFSCV SCWDLRGSLL SLREGQALSV AGGLPSNLSE GLRLGPMNLQ
     DPFDLSHNVA ANVTSRVAGR LQNCCRAAAN YCRSLQYQRR SSRGRDWGLL PLLQPSSPSS
     ILSATPIPLP PASFTQLTAV LAQVLREALG CHIEQGTKRL RSEGGGPGEP PQGGTSKRAK
     LDGQKKSCEE GPEEQQGCAG EHGEDGVEEM VIEVGESVQD WVMRSPGQLG ELPLMTGKHL
     ATREEGQSGT AALAKQGPRG PEAACEGSQA EAEKRVSLTV SWRCALWHRV WQGRRRARRR
     LQQQIKEGGG SGAGSGAEWL ATEAQVTREL RGLSSTEQRP EAEPLLTFVA STSQADQSLT
     VTPLQDSQGL FPDLHHFLQV FLPQALRNLL K
//