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Database: UniProt
Entry: A0A2N6P2F8_BEABA
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ID   A0A2N6P2F8_BEABA        Unreviewed;      1187 AA.
AC   A0A2N6P2F8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, 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   Name=prp22 {ECO:0000313|EMBL:PMB73696.1};
GN   ORFNames=BM221_001120 {ECO:0000313|EMBL:PMB73696.1};
OS   Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS   shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB73696.1, ECO:0000313|Proteomes:UP000235728};
RN   [1] {ECO:0000313|EMBL:PMB73696.1, ECO:0000313|Proteomes:UP000235728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEF-007 {ECO:0000313|EMBL:PMB73696.1,
RC   ECO:0000313|Proteomes:UP000235728};
RX   PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA   Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT   "Characterization of T-DNA insertion mutants with decreased virulence in
RT   the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL   Appl. Microbiol. Biotechnol. 100:8889-8900(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   -!- 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:PMB73696.1}.
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DR   EMBL; MRVG01000001; PMB73696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N6P2F8; -.
DR   OMA; DPMVAPE; -.
DR   Proteomes; UP000235728; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd21691; GH2-like_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:PMB73696.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235728}.
FT   DOMAIN          224..295
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          533..696
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          714..894
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          78..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1187 AA;  133559 MW;  B63B5F71BB8CE388 CRC64;
     MDDFLNLELL SLVSKVTSEL QNHVGVSDKT LAEFLIAQRI ESKNADEFRS KLDGLGADFP
     PSLVDSLDRL VLTMHPRFKG SKGAAEPKEE HHGRSLEEKE KAFSGLALAD GKPSYRDDDG
     DAIDDTLALL EGLEGKARKD KGTRKRSRSP HDESRRRRRD RSRSREGRKR DRFRSRSPSQ
     DRGGQDSRNG YRDSRKSRHG RRDDRYDDLR HAPAPEMDDE PQLNKVYEGH VTGIKDFGAF
     VNLHNVRGRQ DGLVHISKIA AHQRVNHPSD LLEKGKNVWV KVVSVEGKRI SLSMASVDQS
     TGMDKEPQVS FTSGANMEAL GGGGRGFNDV PSGMPRDDIG APRKHKKRMT SPERWEIRQL
     IASGVAKASD YPDLEEEYNA TLRGDGELEL EEDVDIEVRE EEPPFLAGQT KQSLELSPIR
     VVKAPDGSMN RAAMSGTALA KERKELKQQE AEAAKERPKE NLSSQWEDPM ADPQKRQFAS
     DLRNAKTNAG TEDVPEWKRA IVPRNQTLGK RTNLSMKEQR ETLPVYAFRS QLIKAVQENQ
     ILIVVGETGS GKTTQLTQYL AEGGFANDGV IGCTQPRRVA AMSVAKRVAE EVGCKLGEEV
     GYYVRFDDMT GPMTKIKYMT DGMLLREVLG DPDMKRYSVI MLDEAHERTI STDVLFALLK
     KALKRRPDLK VIVTSATLDA DKFSMYFNEC PIFTIPGRTF PVEILYSREP ESDYLDTALV
     TVMQIHLTEP KGDILLFLTG QEEIDTACEV LFERMKALGP GVPELLILPV YAQLPTEMQS
     RIFDPAPPGA RKVVIATNIA ETSITIDEIY YVIDPGFVKQ SAYDPKLGMD SLIVTPISQA
     QANQRAGRAG RTGPGKCFRL YTEAAYQSEM LPTTIPEIQR ANLAHVILML KAMGINDLLH
     FDFMDPPPVN TMLTALEELY ALSALDDEGL LTRLGRKMSD FPMEPSLAKV LITAVDYQCS
     EEMLSIVAML NQSTIFYRPK EKQTQADQKK AKFHDPHGDH LTLLNVYNSW KHSSYSRPWC
     FENFIQDRSM RRAKDVRDQI LRIMERHRHP VVSCGRDTQK VRRALCTGFF RSAARKDPQE
     GYKTLTEGTP VYLHPSSALF GKQAEWVIYH ELVLTTKEYM HWTTAIEPKW LVEAAPTFFK
     VAPTDRLSKR KAQERILPLY NKFAGEDDWR LSAQKRGGRG GGGGTWG
//
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