GenomeNet

Database: UniProt
Entry: A3LS22
LinkDB: A3LS22
Original site: A3LS22 
ID   RRP3_PICST              Reviewed;         484 AA.
AC   A3LS22;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   31-JUL-2019, entry version 61.
DE   RecName: Full=ATP-dependent rRNA helicase RRP3 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P38712};
GN   Name=RRP3 {ECO:0000250|UniProtKB:P38712}; ORFNames=PICST_57234;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: ATP-dependent rRNA helicase required for pre-ribosomal
CC       RNA processing. Involved in the maturation of the 35S-pre-rRNA and
CC       to its cleavage to mature 18S rRNA.
CC       {ECO:0000250|UniProtKB:P38712}.
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         Evidence={ECO:0000250|UniProtKB:P38712};
CC   -!- SUBUNIT: Interacts with the SSU processome.
CC       {ECO:0000250|UniProtKB:P38712}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN65488.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000497; ABN65488.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001383517.2; XM_001383480.1.
DR   SMR; A3LS22; -.
DR   STRING; 4924.XP_001383517.2; -.
DR   EnsemblFungi; ABN65488; ABN65488; PICST_57234.
DR   GeneID; 4838114; -.
DR   KEGG; pic:PICST_57234; -.
DR   eggNOG; KOG0330; Eukaryota.
DR   eggNOG; ENOG410XQU7; LUCA.
DR   HOGENOM; HOG000268802; -.
DR   InParanoid; A3LS22; -.
DR   KO; K14777; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); 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; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 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    484       ATP-dependent rRNA helicase RRP3.
FT                                /FTId=PRO_0000285150.
FT   DOMAIN      102    273       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      300    444       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     115    122       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        71     99       Q motif. {ECO:0000305}.
FT   MOTIF       221    224       DEAD box. {ECO:0000305}.
SQ   SEQUENCE   484 AA;  54357 MW;  0EFF6C4840C99EAC CRC64;
     MAIVGSNSVS KKPKHTKRND ARDLAEKIKR NALKKQEQDK KQQLEEESKP ESSQKSKNIV
     EVNPDDEVKF STFSELKLVP ELLEAIQQMK FSKPTPIQSE AIPHALEGKD IIGLAQTGSG
     KTAAFAIPIL QSLWEAQTPY FGLVLAPARE LAYQIKETFD ALGSTMGVRT VCLVGGMDMM
     DQARDLMRKP HIIIATPGRI MDHLEHTKGF SLKMLKYFVM DEADKLLDLE FGPVLDKILK
     QIPSKRTTYL FSATMTNKIE KLQRASLHNP VRVAVSSKYQ TADNLIQSMM LVSDGYKNTY
     LIHLLNEFVG KSIIIFARTR AHTQRTSILC RILGFSAVPL HGDLTQAQRL GSLNKFKSGT
     ANILIATDVA ARGLDIPSVD VVINYDIPTD SKAYVHRVGR TARAGRSGKS ISLVTQYDLE
     MYLRIEQSIQ KKLPKDPSPP KAMLDALHVH VDRAYAEAIR QTKEFHEKTR RGRRGKDDKD
     REEH
//
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