(data stored in ACNUC7421 zone)

SWISSPROT: Q758E3_ASHGO

ID   Q758E3_ASHGO            Unreviewed;      1071 AA.
AC   Q758E3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 113.
DE   SubName: Full=AEL181Cp {ECO:0000313|EMBL:AAS52504.2};
GN   ORFNames=AGOS_AEL181C {ECO:0000313|EMBL:AAS52504.2};
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:AAS52504.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52504.2, 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).
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DR   EMBL; AE016818; AAS52504.2; -; Genomic_DNA.
DR   RefSeq; NP_984680.2; NM_210033.2.
DR   STRING; 33169.AAS52504; -.
DR   EnsemblFungi; AAS52504; AAS52504; AGOS_AEL181C.
DR   GeneID; 4620865; -.
DR   KEGG; ago:AGOS_AEL181C; -.
DR   HOGENOM; HOG000163047; -.
DR   InParanoid; Q758E3; -.
DR   KO; K12598; -.
DR   OMA; CFVCDEK; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031499; C:TRAMP complex; IEA:EnsemblFungi.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004532; F:exoribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008143; F:poly(A) binding; IEA:EnsemblFungi.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:EnsemblFungi.
DR   GO; GO:0043629; P:ncRNA polyadenylation; IEA:EnsemblFungi.
DR   GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0071049; P:nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription; IEA:EnsemblFungi.
DR   GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IEA:EnsemblFungi.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IEA:EnsemblFungi.
DR   GO; GO:0034476; P:U5 snRNA 3'-end processing; IEA:EnsemblFungi.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   InterPro; IPR025696; rRNA_proc-arch_dom.
DR   InterPro; IPR016438; Ski2-like.
DR   InterPro; IPR012961; Ski2_C.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF13234; rRNA_proc-arch; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
DR   PRODOM; Q758E3.
DR   SWISS-2DPAGE; Q758E3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          156..312
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          391..595
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          854..874
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..43
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..68
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  121408 MW;  F7D388B05A8B7EC3 CRC64;
     MDGDLFSVFG EEPKELPELP AEDIEQVPDE HQVETKKRGL SPSSNTKEES QQAESTAKKV
     KKDKKLVDEK KKSEVVPVLA DSFEKEASRE VEASSGLATA DAAQVEENGK MKLRHQVRHQ
     VALPPNYDYK PIGQHIRTNE ARTYPFTLDP FQDTAVSCID RGESVLVSAH TSAGKTVVAE
     YAIAQSLREK QRVIYTSPIK ALSNQKYREL LAEFGDVGLM TGDITINPDA GCLVMTTEIL
     RSMLYRGSEV MREVAWVIFD EVHYMRDKER GVVWEETIIL LPDKVRYVFL SATIPNAMEF
     AEWICRIHSQ PCHIVYTDFR PTPLQHYLFP AHGDGIHLVV DEKGTFREEN FQKAMASISN
     QLGDDSNSAT SKGKRGQTYK GGAAKGDAKG DIYKIVKMIW KKKYNPVIVF SFSKRDCEEL
     ALKMSKLDFN SDEEKDALTK IFNNAISLLP EADRELPQIK HILPLLRRGI GIHHSGLLPI
     LKEVIEILFQ EGFLKVLFAT ETFSIGLNMP AKTVVFTSVR KWDGKQFRWV SGGEYIQMSG
     RAGRRGLDDR GIVIMMIDEK MEPQVAKGMV KGQADRLDSA FHLGYNMILN LMRVEGISPE
     FMLEHSFYQF QNITSMPVME KKMNELSKKL EDIHVDDESN VKDYYDIRQT LDAYNEDVRK
     VMTHPANVLS FLQPGRLIKI NVGGKQDYGW GAVVDFAKRI NKRDPTAVYA DHDSYIVNVV
     VNTMYKDSPL NLLKPFNPVL PEGIRPAADG EKTTCALISI TLDSIQGLGN LRIFMPSDIK
     ADSQKEVVGK TLKEVQRRFP KGIPLLDPIK NMKLEDEEFL KLLKKIEILE SKMNSNPIAN
     SVKLQELYEK YSEKVAMQND IKHLKSKMNE AQAVIQLDDL RRRKRVLRRL GFCSASDIIE
     LKGRVACDIS SGDELLLTEL ILNGNFNELK PEQAAALLSC FAFQERCKEA PRLKPELAEP
     LKAMREVAAK IAKVIKDSKL EIVEKDYVES FRHELMEVVY EWCRGASFTQ ICKMTDVYEG
     SLIRMFKRLE ELIKELIDVS NTIGNVTLKE KMEAALHMIH RDIVSAGSLY L
//

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