ID   TRPT1_BOVIN             Reviewed;         254 AA.
AC   Q3ZBM7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=tRNA 2'-phosphotransferase 1;
DE            EC=2.7.1.160;
GN   Name=TRPT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-254.
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the last step of tRNA splicing, the transfer of the
CC       splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-
CC       ribose 1''-2'' cyclic phosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-phospho-[ligated tRNA] + NAD(+) = ADP-beta-D-ribose
CC         1'',2''-cyclic phosphate + mature tRNA + nicotinamide;
CC         Xref=Rhea:RHEA:23324, Rhea:RHEA-COMP:11106, Rhea:RHEA-COMP:11107,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:76596,
CC         ChEBI:CHEBI:82883, ChEBI:CHEBI:85027; EC=2.7.1.160;
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI03211.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DN524407; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC103210; AAI03211.2; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q3ZBM7; -.
DR   SMR; Q3ZBM7; -.
DR   STRING; 9913.ENSBTAP00000022022; -.
DR   PaxDb; Q3ZBM7; -.
DR   eggNOG; KOG2278; Eukaryota.
DR   InParanoid; Q3ZBM7; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
DR   Gene3D; 1.10.10.970; -; 1.
DR   Gene3D; 3.20.170.30; -; 1.
DR   InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR   InterPro; IPR042081; RNA_2'-PTrans_C.
DR   InterPro; IPR042080; RNA_2'-PTrans_N.
DR   PANTHER; PTHR12684; PTHR12684; 1.
DR   Pfam; PF01885; PTS_2-RNA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; NAD; Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..254
FT                   /note="tRNA 2'-phosphotransferase 1"
FT                   /id="PRO_0000273362"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TN4"
SQ   SEQUENCE   254 AA;  27791 MW;  F18DA8315C9F2820 CRC64;
     MNSFGGRRRE TAGPKGRRAH RPPQDQDRDV QLSKALSYAL RHGALKLGLP MGADGFVPLD
     ALLQLPQFRS FSAEDVQRVV DTNVKQRFAL QPGDPSTGPL IRANQGHSLQ VPELELEPLE
     TPQALPLMLV HGTFRQHWPS ILLKGLSCRG RTHIHLAPGL PGDPGVISGM RPNCEVAVFI
     NGPLALADGI PFFRSTNGVI LTPGNADGVL PPKYFKEALQ LRPTRKPLSL AGNEEKEHQR
     DSKHSSRGRG MTQQ