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Database: UniProt
Entry: M7WVB4_RHOT1
LinkDB: M7WVB4_RHOT1
Original site: M7WVB4_RHOT1 
ID   M7WVB4_RHOT1            Unreviewed;       656 AA.
AC   M7WVB4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=RHTO_01251 {ECO:0000313|EMBL:EMS22036.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS22036.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS22036.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS22036.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(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   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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:0000256|ARBA:ARBA00001556,
CC         ECO:0000256|RuleBase:RU365068};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
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       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC       subfamily. {ECO:0000256|ARBA:ARBA00024357}.
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DR   EMBL; KB722653; EMS22036.1; -; Genomic_DNA.
DR   RefSeq; XP_016273155.1; XM_016414934.1.
DR   AlphaFoldDB; M7WVB4; -.
DR   GeneID; 27365264; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_5_1; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd17942; DEADc_DDX18; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR044773; DDX18/Has1_DEADc.
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   PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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 {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   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          129..157
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          160..336
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          350..519
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           129..157
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        67..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  72212 MW;  5E3FDAE1ECAB7B87 CRC64;
     MSAVAAPVAS TSAATIEAKK RKRKRTHKKS AAASTTDSNA PAPATPAQPA EEDVEPLIEP
     EFEPAAEEED AGKKGKGAKK RKDDGRGDAG PAFEVEHEGQ ADGTQSGDAA SDALALMTGA
     KVAPEPKSRA FSSLDLSEGT RKAIEGMGFK EMTEVQARTI PPLLAGKDVL GAAKTGSGKT
     LAFLIPAIEM LHRLKFKPRN GTGAIVVTPT RELALQIFGV AKELCEHHNQ TFAIVMGGAN
     RKAEAEKLAK GVNLLIATPG RLLDHLQNTK GFVFSNLRAL IIDEADRILE IGFEDEMRQI
     VALLPKENRQ SMLFSATQTT KVTDLARVSL RPGPLYINVD TKSETSTANN LEQGYVVCDS
     DKRFLLLFTF LRKNLKKKVI VFFSSCKSVQ YHGELLNYID VPVLDLHGKQ KQQKRTNTFF
     EFCNAPTGIL LCTDVAARGL DIPKVDWIIQ FDPPDDPRDY IHRVGRTARA GKQGKSLLFL
     LPSELGFLRF LKVAKVPLNE YSFPNDKIAN VQGQLEKLIA KNYYLHQSAR DGFRAYIQSY
     ASYSLKTIFD VTQLDLAKVA KAFGFSTPPA VNINVGRSAK GKKRKDHPKA GESSEEENES
     EEEDENERER RAKMARRGGS NQAKRREVEG KKAEKDFYRE PGREKLKNAG GTQWSR
//
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