ID   ELP6_SCHPO              Reviewed;         249 AA.
AC   O74385;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Elongator complex protein 6 homolog;
GN   Name=elp6 {ECO:0000303|PubMed:22768388, ECO:0000312|PomBase:SPBC3H7.10};
GN   ORFNames=SPBC3H7.10;
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   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).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=22768388; DOI=10.1016/j.celrep.2012.04.001;
RA   Bauer F., Matsuyama A., Candiracci J., Dieu M., Scheliga J., Wolf D.A.,
RA   Yoshida M., Hermand D.;
RT   "Translational control of cell division by Elongator.";
RL   Cell Rep. 1:424-433(2012).
RN   [4]
RP   REVIEW.
RX   PubMed=29332244; DOI=10.1007/s00018-018-2747-6;
RA   Dalwadi U., Yip C.K.;
RT   "Structural insights into the function of Elongator.";
RL   Cell. Mol. Life Sci. 75:1613-1622(2018).
CC   -!- FUNCTION: Component of the elongator complex which is required for
CC       multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC       uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC       (5-carbamoylmethyl uridine) (PubMed:22768388). The elongator complex
CC       catalyzes formation of carboxymethyluridine in the wobble base at
CC       position 34 in tRNAs (PubMed:29332244). {ECO:0000250|UniProtKB:Q04868,
CC       ECO:0000269|PubMed:22768388, ECO:0000303|PubMed:29332244}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000269|PubMed:22768388}.
CC   -!- SUBUNIT: Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:Q04868}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ELP6 family. {ECO:0000305}.
CC   -!- CAUTION: The elongator complex was originally thought to play a role in
CC       transcription elongation. However, it is no longer thought to play a
CC       direct role in this process and its primary function is thought to be
CC       in tRNA modification. {ECO:0000305|PubMed:29332244}.
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DR   EMBL; CU329671; CAA20306.1; -; Genomic_DNA.
DR   PIR; T40405; T40405.
DR   RefSeq; NP_595765.1; NM_001021666.2.
DR   AlphaFoldDB; O74385; -.
DR   SMR; O74385; -.
DR   BioGRID; 277495; 90.
DR   STRING; 4896.SPBC3H7.10.1; -.
DR   MaxQB; O74385; -.
DR   PaxDb; O74385; -.
DR   EnsemblFungi; SPBC3H7.10.1; SPBC3H7.10.1:pep; SPBC3H7.10.
DR   GeneID; 2540979; -.
DR   KEGG; spo:SPBC3H7.10; -.
DR   PomBase; SPBC3H7.10; elp6.
DR   VEuPathDB; FungiDB:SPBC3H7.10; -.
DR   eggNOG; KOG4723; Eukaryota.
DR   HOGENOM; CLU_1129634_0_0_1; -.
DR   InParanoid; O74385; -.
DR   OMA; CISCRPL; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:O74385; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0033588; C:elongator holoenzyme complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; IMP:PomBase.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IGI:PomBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR018627; ELP6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR16184; PTHR16184; 1.
DR   Pfam; PF09807; ELP6; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..249
FT                   /note="Elongator complex protein 6 homolog"
FT                   /id="PRO_0000351069"
SQ   SEQUENCE   249 AA;  28173 MW;  9C091616D48A1985 CRC64;
     MSSLHEHLRP IPEPFSLTLL LGTRETPVTF LFHYYLYHAL KAKESTCFLT FSKTLDEHAI
     SMRKWGMDIK TKKNFFFIDG FSMLFAPISK PSKVQAPETK NHIKSVFAPV IQCVEENDFE
     FENSTIIIED IDILQSTHAL DSTKIQQAIL ELRKCFSRVI VNVTLGAPLP QQKSLGSSIG
     HMATRCISCR PLTSGSARRI TGFLRLSRMP NHFRSGICET PEDDDKELLY EVTEAGAKVY
     SKGQVTLQL