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Database: UniProt
Entry: R7SKE6_DICSQ
LinkDB: R7SKE6_DICSQ
Original site: R7SKE6_DICSQ 
ID   R7SKE6_DICSQ            Unreviewed;       397 AA.
AC   R7SKE6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=DICSQDRAFT_183742 {ECO:0000313|EMBL:EJF56614.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF56614.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF56614.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF56614.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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       {ECO:0000256|ARBA:ARBA00024310}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX48/FAL1
CC       subfamily. {ECO:0000256|ARBA:ARBA00037945}.
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DR   EMBL; JH719467; EJF56614.1; -; Genomic_DNA.
DR   RefSeq; XP_007370665.1; XM_007370603.1.
DR   AlphaFoldDB; R7SKE6; -.
DR   GeneID; 18841394; -.
DR   KEGG; dsq:DICSQDRAFT_183742; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   OMA; KHGANRV; -.
DR   OrthoDB; 1087080at2759; -.
DR   Proteomes; UP000053319; Unassembled WGS sequence.
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:InterPro.
DR   CDD; cd18045; DEADc_EIF4AIII_DDX48; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF26; EUKARYOTIC INITIATION FACTOR 4A-III; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053319}.
FT   DOMAIN          24..52
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          55..225
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          236..397
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   MOTIF           24..52
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   397 AA;  44850 MW;  8E86E4E63A7F6A8D CRC64;
     MSGGINPGDE KLIFESSEAV PVVSTFDDLG LKEDLLRGIY AYNFEKPSAI QQRAILPIIQ
     GRDVIAQAQS GTGKTATFSI SILQSIDVTV RETQALVLSP TRELATQIQS VLLALGDYMN
     VQCHACIGGT SIGEDIRKLE YGQHVVSGTP GRVFDMIRRR SLRTRNIKML VLDEADELLN
     KGFKDQIYDV YRYLPPATQV VLLSATLPYD VLEMTTKFMT DPIRILVRRD ELTLEGIKQF
     FVAVEKEDWK FDTLCDLYDT LTITQAVIFC NTRRKVDWLT EKMRNANFTV SSMHGEMAQK
     ERDAIMAEFR SGTSRVLITT DVWARGIDVQ QVSLVINYDL PANRENYIHR IGRSGRFGRK
     GVAINFVTVD DVRILRDIEQ YYGTQIDEMP VNAAELI
//
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