ELP2_SCHPO
ID ELP2_SCHPO Reviewed; 760 AA.
AC O94533;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Elongator complex protein 2;
GN Name=elp2; ORFNames=SPCC895.06;
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 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:29332244). The elongator complex
CC catalyzes formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (PubMed:29332244). {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:P42935}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC required for elongator complex assembly.
CC {ECO:0000250|UniProtKB:P42935}.
CC -!- SIMILARITY: Belongs to the WD repeat ELP2 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:Q6IA86}.
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DR EMBL; CU329672; CAA22842.1; -; Genomic_DNA.
DR PIR; T41644; T41644.
DR RefSeq; NP_588047.1; NM_001023039.2.
DR AlphaFoldDB; O94533; -.
DR SMR; O94533; -.
DR BioGRID; 275560; 338.
DR STRING; 4896.SPCC895.06.1; -.
DR iPTMnet; O94533; -.
DR MaxQB; O94533; -.
DR PaxDb; O94533; -.
DR PRIDE; O94533; -.
DR EnsemblFungi; SPCC895.06.1; SPCC895.06.1:pep; SPCC895.06.
DR GeneID; 2538986; -.
DR KEGG; spo:SPCC895.06; -.
DR PomBase; SPCC895.06; elp2.
DR VEuPathDB; FungiDB:SPCC895.06; -.
DR eggNOG; KOG1063; Eukaryota.
DR HOGENOM; CLU_006430_0_0_1; -.
DR InParanoid; O94533; -.
DR OMA; EHTKRVN; -.
DR PhylomeDB; O94533; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:O94533; -.
DR Proteomes; UP000002485; Chromosome III.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISO:PomBase.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR037289; Elp2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44111; PTHR44111; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Protein transport; Reference proteome; Repeat;
KW Transport; tRNA processing; WD repeat.
FT CHAIN 1..760
FT /note="Elongator complex protein 2"
FT /id="PRO_0000316551"
FT REPEAT 49..93
FT /note="WD 1"
FT REPEAT 97..134
FT /note="WD 2"
FT REPEAT 139..182
FT /note="WD 3"
FT REPEAT 189..231
FT /note="WD 4"
FT REPEAT 266..305
FT /note="WD 5"
FT REPEAT 324..363
FT /note="WD 6"
FT REPEAT 368..407
FT /note="WD 7"
FT REPEAT 414..453
FT /note="WD 8"
FT REPEAT 576..615
FT /note="WD 9"
FT REPEAT 622..663
FT /note="WD 10"
FT REPEAT 668..711
FT /note="WD 11"
FT REPEAT 721..760
FT /note="WD 12"
SQ SEQUENCE 760 AA; 84949 MW; 3CD3806D0E76600B CRC64;
MFQYEALHVG CNRIPTAATW SSNLGLIYGA ERLIAVADPF KEINYLMAGH SGRINCVCEL
ATNSEYRSPF ILSGASDKTL RLWQLEEEYF TCIKTIELEA TVNCLCVNEN LVVCGCSNSS
CIVYSWNAEQ RNLTEISRFT CSEIIPLEFA IVKLDHGIIL TVCGSSKKIM VYGSDSAISS
FKLKAVLRGH LDWVRTLSFK KTSGSTATLA SGSQDRYIRL WNISLWGSED EKVSEEFFES
VLSNKPVRFT LGKIDLKIVF DALLMGHEDW VMSVDWHPTK EMILSSSADS SMIVWEPDTN
TGIWVVTGRM GEMASSHGST TATGSAGGFW GGLWNPNGNC VVCWGRTGGW RLWKQDAGQW
LQLPSISGHT KSVKGVAWDP EGKFYLSAGT DQTTRLFARF KKDNAWHEMA RPQIHGYDLT
SISCMPSRIG FLSCADEKVS RVFKFPKTIV RLLYRLCDTN IGEESLPDAA NVPLLGLSNK
ATTASETGTV NAEEVQTPVA DVIGSLNHPP FEEHLQRLLL FPEVEKLFGH GYEVYACAIS
NNGNIAATSC KSQTPEHAVI RLYETQSWNQ QQVLKGHSLT VTTIKFSPDD RYILSAGRDR
LVCLHEQAEN LLDYNNFASI KAHSRIIWDA SWAPKEMGYF FATASRDKFV KFWKINDNKK
ICDVAALQFS DAVTAVDFAP FFHNDELLLA VGTEAGKIFI WRCPRENLTK WYPTRLPDHM
APMESINQIL WKPTFETMGL YSLLIAGEDT SVRLLNVTLG
