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Database: UniProt
Entry: Q74Z73
LinkDB: Q74Z73
Original site: Q74Z73 
ID   HAS1_ASHGO              Reviewed;         504 AA.
AC   Q74Z73;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   16-OCT-2019, entry version 104.
DE   RecName: Full=ATP-dependent RNA helicase HAS1;
DE            EC=3.6.4.13;
GN   Name=HAS1; OrderedLocusNames=AGR333C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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., Poehlmann 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
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 379.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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: ATP-dependent RNA helicase involved in 40S ribosomal
CC       subunit biogenesis. Required for the processing and cleavage of
CC       35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Associates in the nucleolus with the 60S and pre-60S
CC       ribosomal subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC       subfamily. {ECO:0000305}.
DR   EMBL; AE016820; AAS54823.2; -; Genomic_DNA.
DR   RefSeq; NP_986999.2; NM_212061.2.
DR   SMR; Q74Z73; -.
DR   STRING; 33169.AAS54823; -.
DR   EnsemblFungi; AAS54823; AAS54823; AGOS_AGR333C.
DR   GeneID; 4623302; -.
DR   KEGG; ago:AGOS_AGR333C; -.
DR   HOGENOM; HOG000268799; -.
DR   InParanoid; Q74Z73; -.
DR   KO; K13179; -.
DR   OMA; AHHSQTY; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:1990417; P:snoRNA release from pre-rRNA; IEA:EnsemblFungi.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    504       ATP-dependent RNA helicase HAS1.
FT                                /FTId=PRO_0000227956.
FT   DOMAIN       70    246       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      260    430       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      83     90       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        39     67       Q motif.
FT   MOTIF       193    196       DEAD box.
FT   MOTIF       272    288       Bipartite nuclear localization signal.
FT                                {ECO:0000250}.
SQ   SEQUENCE   504 AA;  56109 MW;  D778981F9A40B6BC CRC64;
     MGAQETREDA SGSSKKRQRP ESEVAAESDA AASSTAHAEK FDELNLSSQT LKAIGKMGFT
     KMTQVQARTI PPLMAGRDVL GAAKTGSGKT LAFLLPAIEM LHSLKFKPRN GTGVIVITPT
     RELALQIFGV ARELMEFHSQ TFGIVIGGAN RRQEAEKLAK GVNLLIATPG RLLDHLQNTK
     GFVFKNLKAL VIDEADRILE IGFEDEMKQI IKILPNEDRQ SMLFSATQTT KVEDLARISL
     RPGPLFINVD SEKETSTADG LEQGYVVCDS DKRFLLLFTF LKKFQNKKII VFLSSCNSVK
     YYAELLNYID LPVLELHGKQ KQQKRTNTFF EFCNAERGIL VCTDVAARGL DIPAVDWIIQ
     FDPPDDPRDY IHRVGRTARG TKGKGKSLMF LTPHELGFLR YLKAAKVPLN EYEFPANKIA
     NVQSQLEKLL KTNYELNKIA KDGYRSYLQA YASHSLKTVY QIDKLDLVKV AKSYGFPVPP
     KVNITIGASG KAPAAHKKRK LARD
//
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