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TPT1_YEAST
ID   TPT1_YEAST              Reviewed;         230 AA.
AC   Q12272; D6W1W6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=tRNA 2'-phosphotransferase;
DE            EC=2.7.1.160 {ECO:0000269|PubMed:9148937};
GN   Name=TPT1; OrderedLocusNames=YOL102C; ORFNames=HRE230;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7502582; DOI=10.1002/yea.320111108;
RA   Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT   "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT   the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT   tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL   Yeast 11:1069-1075(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9148937; DOI=10.1074/jbc.272.20.13203;
RA   Culver G.M., McCraith S.M., Consaul S.A., Stanford D.R., Phizicky E.M.;
RT   "A 2'-phosphotransferase implicated in tRNA splicing is essential in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 272:13203-13210(1997).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9915792; DOI=10.1074/jbc.274.5.2637;
RA   Spinelli S.L., Kierzek R., Turner D.H., Phizicky E.M.;
RT   "Transient ADP-ribosylation of a 2'-phosphate implicated in its removal
RT   from ligated tRNA during splicing in yeast.";
RL   J. Biol. Chem. 274:2637-2644(1999).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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:0000269|PubMed:9148937}.
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         Evidence={ECO:0000269|PubMed:9148937};
CC   -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
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DR   EMBL; Z48149; CAA88160.1; -; Genomic_DNA.
DR   EMBL; Z74844; CAA99116.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10682.1; -; Genomic_DNA.
DR   PIR; S51897; S51897.
DR   RefSeq; NP_014539.1; NM_001183356.1.
DR   AlphaFoldDB; Q12272; -.
DR   SMR; Q12272; -.
DR   BioGRID; 34301; 234.
DR   DIP; DIP-2571N; -.
DR   IntAct; Q12272; 6.
DR   MINT; Q12272; -.
DR   STRING; 4932.YOL102C; -.
DR   iPTMnet; Q12272; -.
DR   MaxQB; Q12272; -.
DR   PaxDb; Q12272; -.
DR   PRIDE; Q12272; -.
DR   EnsemblFungi; YOL102C_mRNA; YOL102C; YOL102C.
DR   GeneID; 854051; -.
DR   KEGG; sce:YOL102C; -.
DR   SGD; S000005462; TPT1.
DR   VEuPathDB; FungiDB:YOL102C; -.
DR   eggNOG; KOG2278; Eukaryota.
DR   GeneTree; ENSGT00390000002731; -.
DR   HOGENOM; CLU_052998_1_1_1; -.
DR   OMA; DEEWICA; -.
DR   BioCyc; MetaCyc:G3O-33500-MON; -.
DR   BioCyc; YEAST:G3O-33500-MON; -.
DR   BRENDA; 2.7.1.160; 984.
DR   PRO; PR:Q12272; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12272; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IDA:SGD.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:SGD.
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   1: Evidence at protein level;
KW   NAD; Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..230
FT                   /note="tRNA 2'-phosphotransferase"
FT                   /id="PRO_0000157497"
SQ   SEQUENCE   230 AA;  26196 MW;  7BC2136E127F076F CRC64;
     MRQVLQKDKR DVQLSKALSY LLRHTAVKEK LTIDSNGYTP LKELLSHNRL KTHKCTVDDI
     HRIVKENDKQ RFHIKTLGAD EEWICATQGH SIKSIQPSDE VLVPITEASQ LPQELIHGTN
     LQSVIKIIES GAISPMSRNH VHLSPGMLHA KGVISGMRSS SNVYIFIDCH SPLFFQTLKM
     FRSLNNVYLS SSIPVELIQK VVVKGNLKDE EKLDTLRRIL HERNIPLEKI
 
 
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