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Database: UniProt
Entry: A0A0D2BR54_9EURO
LinkDB: A0A0D2BR54_9EURO
Original site: A0A0D2BR54_9EURO 
ID   A0A0D2BR54_9EURO        Unreviewed;       980 AA.
AC   A0A0D2BR54;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=PV08_01499 {ECO:0000313|EMBL:KIW20920.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW20920.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW20920.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW20920.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847492; KIW20920.1; -; Genomic_DNA.
DR   RefSeq; XP_016241136.1; XM_016375860.1.
DR   AlphaFoldDB; A0A0D2BR54; -.
DR   STRING; 91928.A0A0D2BR54; -.
DR   GeneID; 27328582; -.
DR   VEuPathDB; FungiDB:PV08_01499; -.
DR   HOGENOM; CLU_001832_7_0_1; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT   DOMAIN          342..506
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          531..704
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  111039 MW;  5B1AB5D6EF908C42 CRC64;
     MSEQQYNEPR IKSNKRSNAH RRRRDDIDFE DRWGDEEIAE DEEEAQSDFA ESSSKRVKLS
     DGSGSQQARA RTPPPESAEE KAERERDQDL KERDEFAKRL AKRDEERSKK IVEDRSAPKD
     SVAAQRRALA DDIAARAAAM PDLRVRSRQD YLKKREAERL ALLRKQVAEE QAELRDNPDL
     TRREKEEFAR NKEVLRLAEE RLNIDDHLDG YALPEDYITE KGKIDRRKKE QALYQRYVDR
     DETGRERYVT EHEEWENEQT KRAEAQIKRA EFVDEGDYGY VFDESQQMKF IVAETLGGDL
     GKGMTREQRE MAQRLSAAEA KAKSIEETRK SLPVYQFRDE IIQAVRDHQV LIIVGETGSG
     KTTQLPQYLH EAGFTQGGMK IGCTQPRRVA AMSVAARVAE EMGKRLGNEV GYAIRFEDNT
     SEKTVLKYMT DGMLLRELLT DPELSQYSAL MIDEAHERTV STDIACGLLK DIARARPDLK
     LLISSATMDA RKFQKYFDDA PIFNIPGRRY AVDIHYTAQP EANYLAAAIT TVFQIHITQG
     TGDILVFLTG QEEIEAMEAS LQETARKLGN KIKEMIICPI YANLPTDLQA KIFEPTPAGA
     RKVVLATNIA ETSLTIDGIV YVIDPGFVKE NQYNPRTGME SLVVVPCSRA SAGQRAGRAG
     RVGPGKCFRL YTAQAYKNEL DENTTPEIQR TNLTGVVLLL KSLGINDLLD FDFMDPPSTD
     TLVRAVEQLY ALGALNNAGE LTKIGRQMAE FPTDPMLARS ILAADKYGCV EEVLSIIAML
     GEASALFFRP KDKKIHADSA RARFTNKDGG DHLSLLNVFN EWADSDYSYV WAKENFLQQR
     SLTRARDVRD QLARLCDRVE VDAGKSCGGQ SNIEPIQKAI TAGFFPHSAR LQRDGQSYRT
     VKNGQVVYIH PSGVLIESQP KWLIYHELVL TSKEYMRSCM PLKPEWLIEV APHYYKKKDL
     ETLGVERKVP RGEGKSQSKI
//
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