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 27-MAR-2024, entry version 157. 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-alpha-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7YW4; X-ray; 2.18 A; A=1-230. DR PDBsum; 7YW4; -. DR AlphaFoldDB; Q12272; -. DR SMR; Q12272; -. DR BioGRID; 34301; 235. DR DIP; DIP-2571N; -. DR IntAct; Q12272; 6. DR MINT; Q12272; -. DR STRING; 4932.YOL102C; -. DR iPTMnet; Q12272; -. DR MaxQB; Q12272; -. DR PaxDb; 4932-YOL102C; -. DR PeptideAtlas; Q12272; -. DR EnsemblFungi; YOL102C_mRNA; YOL102C; YOL102C. DR GeneID; 854051; -. DR KEGG; sce:YOL102C; -. DR AGR; SGD:S000005462; -. DR SGD; S000005462; TPT1. DR VEuPathDB; FungiDB:YOL102C; -. DR eggNOG; KOG2278; Eukaryota. DR GeneTree; ENSGT00390000002731; -. DR HOGENOM; CLU_052998_1_1_1; -. DR InParanoid; Q12272; -. DR OMA; YLYHGTV; -. DR OrthoDB; 443016at2759; -. DR BioCyc; MetaCyc:G3O-33500-MONOMER; -. DR BioCyc; YEAST:G3O-33500-MONOMER; -. DR BRENDA; 2.7.1.160; 984. DR BioGRID-ORCS; 854051; 2 hits in 10 CRISPR screens. 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:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:SGD. DR Gene3D; 3.20.170.30; -; 1. DR Gene3D; 1.10.10.970; RNA 2'-phosphotransferase, Tpt1/KptA family, N-terminal domain; 1. DR InterPro; IPR002745; Ptrans_KptA/Tpt1. DR InterPro; IPR042081; RNA_2'-PTrans_C. DR InterPro; IPR042080; RNA_2'-PTrans_N. DR PANTHER; PTHR12684; PUTATIVE PHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR12684:SF2; TRNA 2'-PHOSPHOTRANSFERASE 1; 1. DR Pfam; PF01885; PTS_2-RNA; 1. DR SUPFAM; SSF56399; ADP-ribosylation; 1. PE 1: Evidence at protein level; KW 3D-structure; NAD; Reference proteome; Transferase; tRNA processing. FT CHAIN 1..230 FT /note="tRNA 2'-phosphotransferase" FT /id="PRO_0000157497" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:7YW4" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:7YW4" FT HELIX 121..130 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:7YW4" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:7YW4" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 198..203 FT /evidence="ECO:0007829|PDB:7YW4" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:7YW4" FT HELIX 210..222 FT /evidence="ECO:0007829|PDB:7YW4" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:7YW4" 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 //