GenomeNet

Database: UniProt
Entry: M7WUY7_RHOT1
LinkDB: M7WUY7_RHOT1
Original site: M7WUY7_RHOT1 
ID   M7WUY7_RHOT1            Unreviewed;       794 AA.
AC   M7WUY7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=RHTO_01322 {ECO:0000313|EMBL:EMS21675.1};
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:EMS21675.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS21675.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS21675.1,
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   -!- 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};
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DR   EMBL; KB722654; EMS21675.1; -; Genomic_DNA.
DR   RefSeq; XP_016272794.1; XM_016415004.1.
DR   AlphaFoldDB; M7WUY7; -.
DR   GeneID; 27365335; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_10_1; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EMS21675.1};
KW   Hydrolase {ECO:0000313|EMBL:EMS21675.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          134..338
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          363..543
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..48
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  87409 MW;  864AF026B828419A CRC64;
     MSTATELPKF ITSPRDPPQP ETPPPATCRR RSSPLPPSSG PAPPTSPPRA RVAARTRFPS
     ATASPHKLDS LKRPPPNGTA GSPAPPKKRK LVVFDEEAEQ EANEQQKRKA KEEAQRLRPE
     REKLPVFQGK DAILKGIADN DTVIVLAETG SGKTTQIPQY ILRSDTPCSG PRIVCTQPRH
     VAAISLAQRV SAECGTQTGG LVGYTVRFDN KTSRTTRLTY ATDGALLAEM LGDRDLEAYD
     VVVLDEAHER SLRTNMLMGF LKDIQKRRKE RVRVWKAEQA KSKGKAKANG VVANGEADGK
     KGTDERDPTE LKIVVMSATI DAKRFSDFFD RAPVLYVAGR QHKVKIHYAE EPQPDFLDAA
     LKMVYQIHTR YPPGSILVFL PGQEEIEGLA ASIKSFLPSL QKEYPHAEEL LVTPLYAKLH
     AAEQAKAFLP SPPRTRKVIL ATNIAETSVT IPGVKYVVDC GLAKEKRYHA GTGIDSLVTE
     SISQSSAKQR AGRAGRETDG FCFRLYTEAT YNGLEKRSQP EIQRVSLTFA ILHLLASGQD
     DVFKFSFMDP PDVESIKFAL LTLIGLNALD KRGKITPLGR QMAQLPLDPV YARVLAASFI
     EGCPREMIDL VSLLGSKDQL LINTSSTRDA ANAARQKFVH RTGDHMMLFN ILRAYEELDG
     KDERKQWCKD NFISFKAMSS VLDARKQLLE RAQRLKLGDP DASAGDEAEP VLNALIGGLF
     ANTALRQEDG SYRHTMTKQL VAIHHSSTLH GKKAPAIIDD ELVLTTKTYA RGISSIEPSQ
     IRSKAPSLFG SSLK
//
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