ID   ELP5_SCHPO              Reviewed;         314 AA.
AC   O94495;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Elongator complex protein 5;
DE   AltName: Full=Protein iki1;
GN   Name=iki1; Synonyms=elp5; ORFNames=SPBC18E5.05c;
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   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, a multiprotein complex
CC       which is required for multiple tRNA modifications, including mcm5U (5-
CC       methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-
CC       thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity).
CC       The elongator complex catalyzes formation of carboxymethyluridine in
CC       the wobble base at position 34 in tRNAs (PubMed:29332244).
CC       {ECO:0000250|UniProtKB:P38874, ECO:0000303|PubMed:29332244}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000303|PubMed:29332244}.
CC   -!- SUBUNIT: Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:P38874}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ELP5 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; CAA22665.1; -; Genomic_DNA.
DR   PIR; T39756; T39756.
DR   RefSeq; NP_595851.1; NM_001021755.2.
DR   AlphaFoldDB; O94495; -.
DR   SMR; O94495; -.
DR   BioGRID; 277340; 76.
DR   STRING; 4896.SPBC18E5.05c.1; -.
DR   MaxQB; O94495; -.
DR   PaxDb; O94495; -.
DR   EnsemblFungi; SPBC18E5.05c.1; SPBC18E5.05c.1:pep; SPBC18E5.05c.
DR   GeneID; 2540822; -.
DR   KEGG; spo:SPBC18E5.05c; -.
DR   PomBase; SPBC18E5.05c; -.
DR   VEuPathDB; FungiDB:SPBC18E5.05c; -.
DR   eggNOG; ENOG502QQIZ; Eukaryota.
DR   HOGENOM; CLU_990979_0_0_1; -.
DR   InParanoid; O94495; -.
DR   OMA; WEPESTF; -.
DR   PhylomeDB; O94495; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:O94495; -.
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:0006400; P:tRNA modification; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR019519; Elp5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR15641; PTHR15641; 1.
DR   Pfam; PF10483; Elong_Iki1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..314
FT                   /note="Elongator complex protein 5"
FT                   /id="PRO_0000343152"
SQ   SEQUENCE   314 AA;  35704 MW;  1C2ABC2D1589A061 CRC64;
     MSKFLLNRCI RDLSPLTVLK DNLQQTAKPI LNYYAKNAAS RGIKVLFISY ETLEKEAPEG
     IDCFLYATSW EKVKSLKELY EHISSWRTQG KQHIVMIDTI NPILNTSISS FTMFFGSVLA
     LGSICFLTSF HKDVTLENYP SYLPPCEVFL DFTSTCTVSL IGMQHLSVEH DAKMRSLPNP
     LLEELQDDKI ISLLGSNCET AIVLHVEFRK KSGRIIKESC VLKNGKLEPY TPFEETARGP
     EPADNQIDFN VSFNLNVSEK ERKERDKVFL PYFSAQMVGS QHKSSFVDEG TIIYHADEAD
     DFDEEEDADE DLLI