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Database: UniProt
Entry: A3LNR6
LinkDB: A3LNR6
Original site: A3LNR6 
ID   HAS1_PICST              Reviewed;         567 AA.
AC   A3LNR6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=ATP-dependent RNA helicase HAS1;
DE            EC=3.6.4.13;
GN   Name=HAS1; ORFNames=PICST_81459;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC       biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC       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 ribosomal
CC       subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CP000496; ABN64372.2; -; Genomic_DNA.
DR   RefSeq; XP_001382401.2; XM_001382364.1.
DR   SMR; A3LNR6; -.
DR   STRING; 4924.XP_001382401.2; -.
DR   EnsemblFungi; ABN64372; ABN64372; PICST_81459.
DR   GeneID; 4836874; -.
DR   KEGG; pic:PICST_81459; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; A3LNR6; -.
DR   KO; K13179; -.
DR   OMA; AHHSQTY; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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); IEA:EnsemblFungi.
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; 2.
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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..567
FT                   /note="ATP-dependent RNA helicase HAS1"
FT                   /id="PRO_0000285142"
FT   DOMAIN          134..310
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          324..484
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         147..154
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COILED          35..88
FT                   /evidence="ECO:0000255"
FT   MOTIF           103..131
FT                   /note="Q motif"
FT   MOTIF           257..260
FT                   /note="DEAD box"
SQ   SEQUENCE   567 AA;  63508 MW;  5F23B328A87C133C CRC64;
     MAKNVNSKAN GKKSGSVKRA LKEKKQPEPE FSDSEDDEVD QEKLVEELDE DFDEVANMLG
     ADVTDPEEKK QSKLERKRKR DEEATAEYTK PEVVDNEDDA QNDKFEDAGL SEPTMRAISD
     MGFKTMTKVQ AKTIPPLLAG KDVLGAAKTG SGKTLAFLIP AIELLYSLKF KPRNGTGVIV
     VSPTRELALQ IFGVARELMA HHTQTFGIVI GGANRRQEAE KLAKGVNLLI ATPGRLLDHL
     QNTQGFVFKN LKALVIDEAD RILEIGFEEE MKQIIKILPK EERQSMLFSA TQTTKVEDLA
     RISLRPGPLY INVVPETAAS TADGLEQGYV VCDSDKRFLL LFSFLKKYSK KKIIVFLSSC
     NSVKYFGELL NYIDLPVLDL HGKQKQQKRT NTFFEFCNAK QGTLVCTDVA ARGLDIPAVD
     WIIQFDPPDD PRDYIHRVGR TARGSNGKGK SLMFLTPSEL GFLRYLKAAN VPLNEYEFPT
     NKIVNIQSQL SKLIKSNYWL HQSAKDGYRS YLQAYASHHL KTVYQIDKLD LVKVAKSFGF
     DVPPKVNITI GASGKSIEKK HKKQKRA
//
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