ID A0A169YF89_9HYPO Unreviewed; 979 AA.
AC A0A169YF89;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=BBO_06637 {ECO:0000313|EMBL:OAA39213.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA39213.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA39213.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA39213.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA39213.1}.
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DR EMBL; AZHA01000023; OAA39213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A169YF89; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000076863; 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:0004386; F:helicase activity; 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 Helicase {ECO:0000313|EMBL:OAA39213.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 293..456
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 481..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 111375 MW; 4FA973F5385FBC85 CRC64;
MGEEREYDGY NPKRRRLDGA HSNNRFRKDP RGSTPRAQSR YAPTPPRQQE NEQQPPDEDW
KVLDRDWYMQ DEFGGHAFGD ETHNPFASYE LSTAEALQLE SAQAEKMTSR YDARQEQRRK
ENDAWETNRM LVSGVAQRRD MASDFDDQEA TRVHLLVHEL RPPFLDGRTI FTKQLDPVPA
VRDYQSDMAV FSRKGSKAVK EARQQRERQK QAQQATSLAG TALGNIMGAK EDDGDSALPA
PVEADTETAN RKGGNKFSSH MKKAEGASDF SRSKTLREQR EFLPAFAVRE ELLRVIRENQ
VTIVIGETGS GKTTQLTQFL YEDGYAKTGM IACTQPRRVA AMSVAKRVAE EMDVELGTTV
GYSIRFEDVT SKDTEIKYMT EGILLQHSLT EPDLDRYSCI IMDEAHERAL NTDILFGLFK
KILSRRRDLK LIVTSATMNS RRFSEFFGNA PEFTIPGRTF PVDVMFHRSP VEDYVDQAVQ
QVLAIHVSMD PGDILVFMTG QEDIEITCEL VQKRLDALND PPKLSILPIY SQMPADLQSK
IFERAEAGVR KCVVATNIAE TSLTVDGIKY VVDAGYSKMK VYNPKMGMDT LQITPISQAN
VSQRSGRAGR TGPGKAFRLF TEKAFKEELY LQTIPEIQRT NLANTVLMLK SLGVKDLLEF
DFMDPPPQDT ISTSMFDLWA LGALDNLGEL TEIGRKMSAY PMDPSLAKLL IMAAHYGCSE
EMITIVSMLS VPNVFYRPKE RQDEADTQRE KFWVHESDHL TYLQVYQAWK AHGFSDGWCV
KHFLHSKSLR RAKEIREQLL DIARMQKMEL ASCGMDWDMI RRCICSGYYH QAARYKGSGE
YINLRTNLPV QLHPTSALYA GHPPDYVVYH ELVLTSKVYV STVTAVDPHW LADMGGVFYS
IKEKGYSARD KRITETEFNR KMEIEAKMAE DKRREELRLQ DEAERANQAK KKVNSADGKK
FVTQGAVKKP LVKRRGRGF
//
