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
//