ELP2_DICDI
ID ELP2_DICDI Reviewed; 901 AA.
AC Q86H45; Q552Y9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Elongator complex protein 2;
DE Short=ELP2;
GN Name=elp2; ORFNames=DDB_G0275651;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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). The elongator complex catalyzes formation
CC of carboxymethyluridine in the wobble base at position 34 in tRNAs.
CC {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- SUBUNIT: Component of the elongator complex.
CC {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus
CC {ECO:0000250|UniProtKB:Q6IA86}.
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; AAFI02000013; EAL69576.1; -; Genomic_DNA.
DR RefSeq; XP_643531.1; XM_638439.1.
DR AlphaFoldDB; Q86H45; -.
DR SMR; Q86H45; -.
DR STRING; 44689.DDB0231759; -.
DR PaxDb; Q86H45; -.
DR EnsemblProtists; EAL69576; EAL69576; DDB_G0275651.
DR GeneID; 8620113; -.
DR KEGG; ddi:DDB_G0275651; -.
DR dictyBase; DDB_G0275651; elp2.
DR eggNOG; KOG1063; Eukaryota.
DR HOGENOM; CLU_006430_2_0_1; -.
DR InParanoid; Q86H45; -.
DR OMA; EHTKRVN; -.
DR PhylomeDB; Q86H45; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q86H45; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033588; C:elongator holoenzyme complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:dictyBase.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 6.
DR InterPro; IPR037289; Elp2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44111; PTHR44111; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..901
FT /note="Elongator complex protein 2"
FT /id="PRO_0000327784"
FT REPEAT 11..50
FT /note="WD 1"
FT REPEAT 53..104
FT /note="WD 2"
FT REPEAT 113..155
FT /note="WD 3"
FT REPEAT 173..214
FT /note="WD 4"
FT REPEAT 225..274
FT /note="WD 5"
FT REPEAT 327..377
FT /note="WD 6"
FT REPEAT 387..426
FT /note="WD 7"
FT REPEAT 435..474
FT /note="WD 8"
FT REPEAT 495..535
FT /note="WD 9"
FT REPEAT 653..697
FT /note="WD 10"
FT REPEAT 700..739
FT /note="WD 11"
FT REPEAT 749..788
FT /note="WD 12"
FT REPEAT 796..844
FT /note="WD 13"
FT REPEAT 859..897
FT /note="WD 14"
FT REGION 571..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 100804 MW; 7A9F21E538983317 CRC64;
MNVSSDVDFI SVGCNCLGDC LVWGQNKLAA YGAQNFIALF DPIQSKVLAT LPGHKDRVNH
ICWVPNINEE YKNRYSSYEN ELLSCSSDNT IISWKQIKGG LNYQYKVVEV LKGHSDSVTN
ISVLDFPDGS LLMCSTSADN TVKLWRRESL TKENIDTDTL PKWECIQTID FTPKCMECSS
LAFIPGTTIP LLAVGGLEPK IHIYIQNLDS TTATLQFKKL MSLQGHQDWI RSLSFKTINE
GEGEGEEEEL ILASSSQDFK IRLWKISKFT AEKQKQQQLD ESGNGGANLL GSLSTQLSGV
TSLSTKGYLF NCNSVKYIIL LDAVLSGHDD WVYSIHWSPA RRDQETGKKI QEQMLISASM
DKTAIVWRPD RTTGIWIDES RVGDMGGNIL GQYGAVFSPC SQYILSHGYN GAFHFWKQNT
NQKSSFWEPQ IVVSGHFGPV QDLMWSPDYS YFISCSTDRT LRLFSEWKRN NNNNNLENNK
EQQIISWNEI ARPQIHGYDL ECFTFINKKT HVIVSGAEEK IMRAFVGSQN FVDTLLNISK
VQPVNDGTQR PLAANQPSLG LSNKPYFTGG SDYNENIDNN NNNNNNNGNG EENTEDSIKM
KMGGGDEGGG GEGMDTGYFE DEIPFNPEVL SEPPFEEHLL QSSLWPEIHK FYGHGNEIVA
VACSADGMYL ASTCRASSAD QATVRIWNVS NWKECANLKG HTLTVVNLSF SHNSKYLLGV
SRDRMWTLWE RSASNSEEPF VKVISAPKSH GRIIWSGSWS HDDKFFATGA RDKLVKVWNL
DNIKDIKNAC ASTLPAFGSG VTCVEFAPKS SKFTGEHGDH LLAVGEDDGK ITIWKSTTST
SNPKSLDWTC VHTISPLISH TLDVRRIRWR DTPTINGNSL TYQIVTCSVD HSVRIFNIKF
D