ELP1_SCHPO
ID ELP1_SCHPO Reviewed; 1253 AA.
AC O59704;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Elongator complex protein 1;
GN Name=elp1 {ECO:0000312|PomBase:SPBC36.07};
GN Synonyms=iki3 {ECO:0000303|PubMed:22768388, ECO:0000312|PomBase:SPBC36.07};
GN ORFNames=SPBC36.07;
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). ELP1 binds
CC to tRNA, mediating interaction of the elongator complex with tRNA (By
CC similarity). {ECO:0000250|UniProtKB:Q06706,
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: Homodimer. Component of the elongator complex.
CC {ECO:0000250|UniProtKB:Q06706}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ELP1/IKA1 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:O95163}.
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DR EMBL; CU329671; CAA19055.1; -; Genomic_DNA.
DR PIR; T40302; T40302.
DR RefSeq; NP_595335.1; NM_001021243.2.
DR AlphaFoldDB; O59704; -.
DR SMR; O59704; -.
DR BioGRID; 277532; 89.
DR IntAct; O59704; 1.
DR STRING; 4896.SPBC36.07.1; -.
DR iPTMnet; O59704; -.
DR MaxQB; O59704; -.
DR PaxDb; O59704; -.
DR PRIDE; O59704; -.
DR EnsemblFungi; SPBC36.07.1; SPBC36.07.1:pep; SPBC36.07.
DR GeneID; 2541017; -.
DR KEGG; spo:SPBC36.07; -.
DR PomBase; SPBC36.07; -.
DR VEuPathDB; FungiDB:SPBC36.07; -.
DR eggNOG; KOG1920; Eukaryota.
DR HOGENOM; CLU_001477_0_0_1; -.
DR InParanoid; O59704; -.
DR OMA; DMNILHD; -.
DR PhylomeDB; O59704; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:O59704; -.
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:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; 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 InterPro; IPR006849; Elp1.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12747; PTHR12747; 1.
DR Pfam; PF04762; IKI3; 1.
DR PIRSF; PIRSF017233; IKAP; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; tRNA processing.
FT CHAIN 1..1253
FT /note="Elongator complex protein 1"
FT /id="PRO_0000339337"
FT REGION 830..1253
FT /note="Mediates dimerization"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT REGION 1126..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1155
FT /note="Required for binding to tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06706"
SQ SEQUENCE 1253 AA; 141607 MW; 47698F966D9E2FE3 CRC64;
MKNLVTHLHH VFPNVNGSIK ALAFNSISDK IYVVCGLDNE NPGIEIYEIS ENDDVSKLVE
FDSPSFVSDN GDIDEIQSMQ FLGEPMAICL SLKGGDIVMV KVDPSPEEAP WEIIGNVENG
IVASCWSTDE QVFCIITGGD TILFMTKNFD IISETSLSDA DLNEFNKHIS VGWGRSETQF
RGKRVRAKLR DPTLPEKIDE GKLSDVDDGK TYICWRGDSQ YVSINRLEKG PRRAIRVYSR
EGLLDSISEP QDGQQSLLSW KPSGSVLATI KSDSSDNSSK VIFFERNGLR HGEFSLRRRE
DEKYTGLAWN VSSSILAVST ENSVMLWTTG NYHWYLKKEI NIPQNALISW HPEHANTLYI
TGKNHIEKVV FDLKYVTEFS TSPNDFGLIP VIDGSSLLVT PLSLCNIPPP MCRYKLSLDY
NVQMTSINAT SDMLFAADDR RLTAFTFNSQ EDIAKFGEFD ISTYAEGLNF KSLLGLSGNQ
VLLLADGTNN CSKFFVFQCD EDNESLKLLA SESFESCILN ASYCSEMLFF QTSSGKLISY
NLNVKSIESI SLSFPKPCSD FVVVPVHETF VPIGLTSYGR LYAEQRLLST GVLSFFCTER
FVLFTTTKNL LKFVHLVSTV DDLQVVEDDA VDRHDERCRV VERGSKIVAS MPSKMAVVLQ
MPRGNLETIY PRIMVLDGVR TYIKALKYGD AFKVCRTHRL DLNILFDYDP DLFLKNIPVF
VDGLYRVDYL DLFLTSLKPE NVTTGMYSDT SKSQSQQSVT TIDNKVNLLC KIIREHLTSK
YGDTHFQAII TSYLCESPPK IEAALGMISG LIKAQSETVD LAIEHMCFLV DVNMLFDHAL
GLYDLKLALL IAQQSQKDPR EYVPFLHEFQ KQESLRRKFN IDCYLKRYER ALGHLKEMEN
AFDEFKNFTI QHKLYPRALE LYKYDKEAQK EVLIIFAQYL RENGKSNEAA IAYESVGKIS
EAIEAYKSAG MWRECLSILQ QTTNSEDLIR ETAEDLASLC IEKREHCDAG SINLLYLSNP
REAVIQMCKG SQYSEAIRIA RATGDSSIYK DLLISVLGES FGEASELVAD FRNQIKSQTE
RILVLREKKK EDPISWMEGT MEDQTPDDIS LASTSLSTNR SLYTQYTKSS NSSKMTRNTS
KNNRRLERKR ARGKKGTVFE EEYLVNSLRR LIARVEEIRP EVHRLLEALV RCNMTTQASE
LQRNFANVIG TIGEKVIPIL SVPVSTFETA LGEQPQAPVV PNVKPFEKLS ILI
