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TPT1_SCHPO
ID   TPT1_SCHPO              Reviewed;         365 AA.
AC   O14045;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative tRNA 2'-phosphotransferase;
DE            EC=2.7.1.160;
GN   ORFNames=SPAC2C4.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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}.
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DR   EMBL; CU329670; CAB16372.2; -; Genomic_DNA.
DR   PIR; T38523; T38523.
DR   RefSeq; NP_594515.2; NM_001019944.2.
DR   AlphaFoldDB; O14045; -.
DR   SMR; O14045; -.
DR   BioGRID; 278069; 1.
DR   STRING; 4896.SPAC2C4.12c.1; -.
DR   iPTMnet; O14045; -.
DR   MaxQB; O14045; -.
DR   PaxDb; O14045; -.
DR   PRIDE; O14045; -.
DR   EnsemblFungi; SPAC2C4.12c.1; SPAC2C4.12c.1:pep; SPAC2C4.12c.
DR   GeneID; 2541572; -.
DR   KEGG; spo:SPAC2C4.12c; -.
DR   PomBase; SPAC2C4.12c; -.
DR   VEuPathDB; FungiDB:SPAC2C4.12c; -.
DR   eggNOG; KOG2278; Eukaryota.
DR   eggNOG; KOG4774; Eukaryota.
DR   HOGENOM; CLU_874815_0_0_1; -.
DR   InParanoid; O14045; -.
DR   OMA; KRNHIHC; -.
DR   PRO; PR:O14045; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; ISS:PomBase.
DR   GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; ISS:PomBase.
DR   GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; ISO:PomBase.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:PomBase.
DR   Gene3D; 1.10.10.970; -; 1.
DR   Gene3D; 3.20.170.30; -; 1.
DR   InterPro; IPR019191; Essential_protein_Yae1_N.
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.
DR   Pfam; PF09811; Yae1_N; 1.
PE   3: Inferred from homology;
KW   NAD; Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..365
FT                   /note="Putative tRNA 2'-phosphotransferase"
FT                   /id="PRO_0000316237"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  41028 MW;  32F645818B1B7997 CRC64;
     MYKNMNSHEL IEESNNSGTP ATKSSSKPTK KIRPRNDLVH YSKALSKVLR HTAKANGLQI
     REDGYIEVDS ILKLPQFRGM GMELLLSIVK GNDKKRFTME EVEGVLYIRA NQGHSIKAVQ
     VPMARIDNAS SIPKVVHGTK KELWPVISKQ GLSRMKRNHI HCATGLYGDP GVISGIRKSC
     TLYIYIDSAK AMQDGVEFYR SENGVILTEG VNGLLSSKYF SRVETSDGEV LLDAKASPKN
     NRSDESDQSD PESIDPFCDN LQALSMHELE LLEEKHSNFG YSEGIIKGKM QVAQSGFDDG
     FKHGSRLGFQ MGKTIGTLKA KLYIFEENEQ MEILKQELDR LQESAEFHIF VANHKEEILK
     CIREK
 
 
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