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Database: UniProt
Entry: A0A1Y1VJE0_9FUNG
LinkDB: A0A1Y1VJE0_9FUNG
Original site: A0A1Y1VJE0_9FUNG 
ID   A0A1Y1VJE0_9FUNG        Unreviewed;       942 AA.
AC   A0A1Y1VJE0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=BCR36DRAFT_580584 {ECO:0000313|EMBL:ORX57172.1};
OS   Piromyces finnis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX57172.1, ECO:0000313|Proteomes:UP000193719};
RN   [1] {ECO:0000313|EMBL:ORX57172.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT   biomass hydrolysis.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORX57172.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORX57172.1}.
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DR   EMBL; MCFH01000006; ORX57172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1VJE0; -.
DR   STRING; 1754191.A0A1Y1VJE0; -.
DR   EnsemblFungi; ORX57172; ORX57172; BCR36DRAFT_580584.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000193719; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
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   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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193719}.
FT   DOMAIN          254..417
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          439..614
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..78
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..942
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  108388 MW;  4EA70F324B2B9B4C CRC64;
     MEDELNIEEE ESENWENDED RLKWEEEQKR LDREWYNIEE GSTMDETHNP YVEYEEYYQK
     KEEELAKQQA KKMSIRQAQY NQDNNLWETN RMITSGVVQR VEVDMDFDDN QEARIHLLVR
     DLKPPFLDGN IIYTRQLEAV QPIKDPSSDM AVVARKGSRL VRDKRERQER INAQPKSWEL
     TGTKLGNIMG ITDKEQEKEK EKEKQVNDED YKGESKFAEH LKDKSDAVSS FARSKTIREQ
     REFLPVFAVR EELLNVIRDN QVIIIVGETG SGKTTQLTQY LHEDGYSKHG IIGCTQPRRV
     AAMSVAKRVS EETMSKLGET VGYAIRFEDC TSEKTVIKYM TDGVLLRETL KEPDLDKYSA
     IILDEAHERS LHTDVLMGLL KRIIARRRDL KLIVTSATMN SKQFSDFFGG VPIFEIPGRT
     FPVDVVFSKT PCEDYVDSAV KQILSIHLSQ PTGDILVFMT GQEDIEITAQ VTAERLEQLD
     EPPPLSILPI YSQLPADLQA KIFEKAENNA RKCIIATNIA ETSLTVDGIM YVIDSGYCKL
     KVFNPKIGMD SLQITPISQA NANQRSGRAG RTGAGTCYRL FTEAAFLHEM FMNTIPEIQR
     TNLSNVVLLL KSLGVENLLH FDFMDPPPQD NILNSMYQLW VLGALGNTGE LTESGKKMNE
     FPCDPSLSKM IIMSEELGCT AEILTIVSML SVPNVFYRPK ERAEESDAAR EKFFVPESDH
     LTLLHVYTQW KANGYRDSWC VQHFIHPKAM RKAREVRQQL LDIMKSQRIP LTSCGTDWDI
     VRKCICSSYF HQAAKQKGIG EYINMRTGMP CHLHPTSALY GLGYVPDYIV YHELVMTSKE
     YMQCVTSVDP YWLAELGPMF YSIKEQNFSQ TEKRRKDIKE TKSMEEELRH VQEVNRKKEI
     ERRKTEQIPR SIIATPGKFA TPRPRARTSR TPRLKTPRHY GI
//
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