DPH7_SCHPO
ID DPH7_SCHPO Reviewed; 326 AA.
AC O74865;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Diphthine methyltransferase;
DE EC=3.1.1.97;
DE AltName: Full=Diphthamide biosynthesis protein 7;
DE AltName: Full=WD repeat-containing protein rrt2;
GN Name=rrt2; ORFNames=SPCC18.15;
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).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the demethylation of diphthine methyl ester to form
CC diphthine, an intermediate in diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in translation
CC elongation factor 2 (eft201 and eft202).
CC {ECO:0000250|UniProtKB:P38332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphthine methyl ester-[translation elongation factor 2] + H2O
CC = diphthine-[translation elongation factor 2] + H(+) + methanol;
CC Xref=Rhea:RHEA:42656, Rhea:RHEA-COMP:10172, Rhea:RHEA-COMP:10173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:79005, ChEBI:CHEBI:82696; EC=3.1.1.97;
CC Evidence={ECO:0000250|UniProtKB:P38332};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DPH7 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21429.2; -; Genomic_DNA.
DR PIR; T41158; T41158.
DR RefSeq; NP_588394.2; NM_001023385.2.
DR AlphaFoldDB; O74865; -.
DR SMR; O74865; -.
DR STRING; 4896.SPCC18.15.1; -.
DR iPTMnet; O74865; -.
DR MaxQB; O74865; -.
DR PaxDb; O74865; -.
DR PRIDE; O74865; -.
DR EnsemblFungi; SPCC18.15.1; SPCC18.15.1:pep; SPCC18.15.
DR GeneID; 2539212; -.
DR KEGG; spo:SPCC18.15; -.
DR PomBase; SPCC18.15; -.
DR VEuPathDB; FungiDB:SPCC18.15; -.
DR eggNOG; KOG0280; Eukaryota.
DR HOGENOM; CLU_036100_0_0_1; -.
DR InParanoid; O74865; -.
DR OMA; HESMCYG; -.
DR UniPathway; UPA00559; -.
DR PRO; PR:O74865; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0061685; F:diphthine methylesterase activity; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; ISO:PomBase.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISO:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..326
FT /note="Diphthine methyltransferase"
FT /id="PRO_0000372416"
FT REPEAT 65..105
FT /note="WD 1"
FT REPEAT 113..152
FT /note="WD 2"
FT REPEAT 155..195
FT /note="WD 3"
FT REPEAT 293..326
FT /note="WD 4"
SQ SEQUENCE 326 AA; 37040 MW; 9AA35ABD0B9DE737 CRC64;
MSETGIIPKS TDYTDWPADV CKYSQVFEDV LVVGTYMLDE STKLRHGKLV LYDTKEDVLK
RVFDMHCDAI LDFKWSPHDA SVLAVAHSTG HVSFYRHQFR AELMFLRGIK VADSSVLMLS
LDFSDSGKEL AVSMSNGSVL IIDIDSGVIK NKWKEHDYEA WTCHYSRQDN NLLYSGGDDA
ALVCYDQRIP NSCIWRDIQV HHSGVVSILS RAPFGPYIAT GEYGDFMHTL DTRNIGKPLF
SANLGGGVWR LEHMETTENY HKVLGILMHR GAQVLRISND FSSIDASKRI FKEHESMCYG
GDWRHTDGLL ATCSFYDKRV CLWEDI
