(data stored in SCRATCH zone)

SWISSPROT: Q757G6_ASHGO

ID   Q757G6_ASHGO            Unreviewed;      1324 AA.
AC   Q757G6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 102.
DE   RecName: Full=Elongator complex protein 1 {ECO:0000256|PIRNR:PIRNR017233};
GN   ORFNames=AGOS_AER047C {ECO:0000313|EMBL:AAS52731.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52731.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52731.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the RNA polymerase II elongator complex, a
CC       multiprotein complex associated with the RNA polymerase II (Pol II)
CC       holoenzyme, and which is involved in transcriptional elongation.
CC       {ECO:0000256|PIRNR:PIRNR017233}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR017233}.
CC       Nucleus {ECO:0000256|PIRNR:PIRNR017233}.
CC   -!- SIMILARITY: Belongs to the ELP1/IKA1 family.
CC       {ECO:0000256|PIRNR:PIRNR017233}.
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DR   EMBL; AE016818; AAS52731.2; -; Genomic_DNA.
DR   RefSeq; NP_984907.2; NM_210261.2.
DR   STRING; 33169.AAS52731; -.
DR   EnsemblFungi; AAS52731; AAS52731; AGOS_AER047C.
DR   GeneID; 4621109; -.
DR   KEGG; ago:AGOS_AER047C; -.
DR   HOGENOM; HOG000188454; -.
DR   InParanoid; Q757G6; -.
DR   KO; K11373; -.
DR   OMA; QSQKDPR; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033588; C:Elongator holoenzyme complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000049; F:tRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IEA:EnsemblFungi.
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;
DR   PRODOM; Q757G6.
DR   SWISS-2DPAGE; Q757G6.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR017233};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR017233};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transcription {ECO:0000256|PIRNR:PIRNR017233};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR017233}.
FT   REGION          1189..1219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1133..1157
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1203..1217
FT                   /note="Basic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1324 AA;  148815 MW;  B3687461D926E65B CRC64;
     MRNLVSLNKG SLQPSSEAHP NLGLYASCFD TLSDSVTCVL GAADVGAIVV HQYMKSGAVR
     ELASFFTQDY EDELVSFAHF ADVNQLVFVF AHGDIMMATY GDEGAGLDAT VVEIVGSIED
     GIAAAEWSHD EETLALVTGG RSVVLLSRQF EPVADIGLEL DDLKLSKNVT VGWGKKETQF
     RGKGARAMER EALQSLKASG LVGNELRDPT MPYMVDSGAI TELDPRTVGI SWRGDCEYFV
     VSTIETVQDP DDDSATLERR ALRVYSRHGK LDSASEPVDG LEHALAWRPQ GSLIASIQRK
     VNVPGNESLD LVFFERNGLR HGEFETRLAI DERIKSLAWN ASSDILSIAL EDRIQLWTSK
     NYHWYLKQEL YTECTKFVKW HPEKDFTLMY GDGDTVNVVD FAYKMIRGPT FEPNDCGMTV
     VIDGRTVNIT PFAMANVPPP LSYRDFDAPD NVLDAAVGLS NTVFAAVTRE ALVVASIESL
     ANMKSGRHPI IASTFQKHLF ATELDTIRQV AFINDSVVGI LLDSGQLSRI ALVNIQDPIQ
     PELIKVVDTY TKVVLVKSSF DYSTLVYETR DGTVVQLDAE GGTVEITKFP QLVNDFCVKR
     ILTDGKTEWQ PAESKLVAFG LTSSGKLYAD SVQLASAVIS MDITDELLLF TSAQHYLQFV
     HLNTPEFKPL PTLEGDIMDE RIRSIERGSI LINIIPSKAA VVLQAPRGNV ETIYPRIMVL
     AEVRKYIGLK RYKDAFVICR THRIHLDILH DYAPDLFYAN LKTFVDDIER VDYLDLFISC
     LVEEDVTVTK YKETLNMSTD AVFDVAPPPP TEMEEYIKKK SFNPLKSKVN KICQVLLEVL
     LGTAQYKAKY LQTIVTCYAC QNPPKVKDAL ALISQLRDEE AKDSTVTYLC FLQDVLFVYK
     EALALYDVNM ALLVAQKSQM DPREYLPFLQ NLNEQEPLRR KFMIDDHLKN YEMALTHLVG
     IDEPTGAVSD ETREYIQQHE LYKKALDLYR YNTQLQNSVY AIYGAHLASK QEYNEAGIIY
     ELLGNWEKAM EVFTMGNKWS PALAIASQHF PDRVLDIATE LVDSLQYEHR YAEAAHVELK
     FMKNVRSAVS LYCKAYDYEQ GILLCITEGT PELINELVDP ALGDGFSVLA ELLADCKGQI
     NSQLRRLREL RAKKEEDPYA FYGQETEEAD DVSIAASETS TKESFFTRYT GKTGGTAKTG
     ASRRTAKNKR REERKRARGK KGTIYEEEYL VKSIGRLIDR LKQTLPDGVK LVDALLRRNM
     REQAYQVQKG FVSMEALLKA NIVEIYNISE KDRERIDDNG NVYQLPVIPV PEIPAFPVRQ
     IIDY
//

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