ID   ELP4_SCHPO              Reviewed;         361 AA.
AC   Q9USP1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Elongator complex protein 4;
GN   Name=elp4 {ECO:0000303|PubMed:22768388, ECO:0000312|PomBase:SPCC11E10.06c};
GN   ORFNames=SPCC11E10.06c;
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, 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) (PubMed:22768388).
CC       The elongator complex catalyzes formation of carboxymethyluridine in
CC       the wobble base at position 34 in tRNAs (PubMed:29332244).
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:Q02884}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ELP4 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:0000250|UniProtKB:Q96EB1}.
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DR   EMBL; CU329672; CAB57848.1; -; Genomic_DNA.
DR   PIR; T40857; T40857.
DR   RefSeq; NP_588202.1; NM_001023192.2.
DR   AlphaFoldDB; Q9USP1; -.
DR   SMR; Q9USP1; -.
DR   BioGRID; 275561; 52.
DR   STRING; 4896.SPCC11E10.06c.1; -.
DR   iPTMnet; Q9USP1; -.
DR   MaxQB; Q9USP1; -.
DR   PaxDb; Q9USP1; -.
DR   EnsemblFungi; SPCC11E10.06c.1; SPCC11E10.06c.1:pep; SPCC11E10.06c.
DR   GeneID; 2538987; -.
DR   KEGG; spo:SPCC11E10.06c; -.
DR   PomBase; SPCC11E10.06c; elp4.
DR   VEuPathDB; FungiDB:SPCC11E10.06c; -.
DR   eggNOG; KOG3949; Eukaryota.
DR   HOGENOM; CLU_040685_0_0_1; -.
DR   InParanoid; Q9USP1; -.
DR   OMA; CHTFDLT; -.
DR   PhylomeDB; Q9USP1; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q9USP1; -.
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:0033588; C:elongator holoenzyme complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
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   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008728; Elongator_complex_protein_4.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12896; PTHR12896; 1.
DR   Pfam; PF05625; PAXNEB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..361
FT                   /note="Elongator complex protein 4"
FT                   /id="PRO_0000339338"
FT   REGION          93..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   361 AA;  40385 MW;  F2BE682779D85CFB CRC64;
     MSFKRKAAPQ IAPTNLPTGV RLSSKDARWI TSSGSSSFDY YLSGGIPMKS LLVIEEDSMD
     YASVLLKFFA AEGLKQDHVI WLGPSIGEMW FRQLPGDSDR PNKNENSAGE DNHSSPPSKN
     PQQERMKIAW RYEQVSKTKA PTLDMIPPGY THSFDLSKNL IVKSDMKYAV SPFPLETGSN
     PYAPVIESLT RFLSTLTPGT VCRLVLPSIL SPAFYSIRAT HPQHFIRFIH TLSSLIKCTT
     SVHLICMCSV PSTLFSRDCE QIFWLENLAS AVFSLHPFPV KETVNGLVTQ PLGLFRIHKL
     PLALPFTNHA NSNEAGDLSF TVSKRRFTIE PWVLPPLDDE QKDTKISNTN PQKQPVKSLD
     F