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Database: UniProt
Entry: S9W393_SCHCR
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Original site: S9W393_SCHCR 
ID   S9W393_SCHCR            Unreviewed;       469 AA.
AC   S9W393;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=ATP-dependent RNA helicase Rrp3 {ECO:0000313|EMBL:EPY52415.1};
GN   ORFNames=SPOG_01740 {ECO:0000313|EMBL:EPY52415.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY52415.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY52415.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000256|ARBA:ARBA00024350}.
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DR   EMBL; KE546989; EPY52415.1; -; Genomic_DNA.
DR   RefSeq; XP_013022298.1; XM_013166844.1.
DR   AlphaFoldDB; S9W393; -.
DR   STRING; 653667.S9W393; -.
DR   EnsemblFungi; EPY52415; EPY52415; SPOG_01740.
DR   GeneID; 25036066; -.
DR   eggNOG; KOG0330; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   OMA; GIGIKCC; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase 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   CDD; cd17954; DEADc_DDX47; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR044765; DDX47/Rrp3_DEADc.
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   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF21; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT   DOMAIN          50..78
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          81..252
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          279..423
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           50..78
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   469 AA;  52527 MW;  7BE732AE2DFB9B1A CRC64;
     MTTDIKKQKK NVKVDGVEDE GFKEETEKKT TSASNSSSED EDQKKEAPPK TFRELGVIEE
     LCDACEKLGY KDPTPIQREA IPTALNKRDV IGLAQTGSGK TAAFAIPVIQ ELWDNPSAYY
     AVVLAPTREL AYQISEQFEA LGGAIGVRSV VIVGGMDMVS QAVALSKKPH ILVCTPGRLM
     DHLENTKGFS LRNLKYLIMD EADRLLDMDF GPIIDKFLKV IPKERRTLLF SATMTSKVEK
     LQRASLHNPV RVAVSSKFST VDTLIQRYLF FPFKHKDTYL VYLVNELAGN TILVFARTVH
     DTQRLAILLR SLGFSAIPLH GQLSQSNRLG ALNKFKSGSR SIMVATDVAA RGLDIPLVDV
     VVNYDIPTDS KAYVHRVGRT ARAGRAGKSV ALVTQYDLEP FLRIEAAIGK KMQEYEHEKD
     AVFLLSERVD EAQREAAIQM KELQDRRRSK NNFRAKRKHD DLDREEQVS
//
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