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Database: UniProt
Entry: E9E3Y7_METAQ
LinkDB: E9E3Y7_METAQ
Original site: E9E3Y7_METAQ 
ID   E9E3Y7_METAQ            Unreviewed;       763 AA.
AC   E9E3Y7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=MAC_04585 {ECO:0000313|EMBL:EFY89399.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY89399.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY89399.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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};
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DR   EMBL; GL698500; EFY89399.1; -; Genomic_DNA.
DR   RefSeq; XP_007810925.1; XM_007812734.1.
DR   AlphaFoldDB; E9E3Y7; -.
DR   STRING; 655827.E9E3Y7; -.
DR   GeneID; 19248896; -.
DR   KEGG; maw:MAC_04585; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; E9E3Y7; -.
DR   OMA; KVKVWRH; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
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; cd17917; DEXHc_RHA-like; 1.
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; 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:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EFY89399.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002499}.
FT   DOMAIN          106..295
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          326..503
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   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  85488 MW;  90317D8388C106E9 CRC64;
     MSPGNTTQRP SKRRKTQSSS QTLRIGGKII PLDGYLTSSS EKADVKPEKP SESIADHETK
     TSPSTEILKK HHETKSIAAR GIEDVALLKT RRELPIWQYR HQIQEALLGP KNEVLILVGE
     TGSGKSTQVP QFLYRESWCK RRKVRVPSPE KEIYVGGCIA ITQPRRVAAT TLAHRVSQEA
     GTPLVKGRKE GLVGYSVRFD HQIPKGTKIK FLTEGTLLQE LLRDPYLRRY NAIIVDEIHE
     RSLDVDLLVG FLKQILSSDQ KMRGGVPLKV VIMSATADVD VLESFFNDSS IYSDPRLVKV
     LRIEGRQFPV EVTHEPQPVA DIQDSLVKRI FKIHMEEPLP GDVLAFLTGQ EEIESAQKLI
     EEYATTLASN VPKVKVFPLY GQLSIDGQRE AFLPAQTKFT RKIVLATNIA ETSVTVPGVR
     YVVDGGKAKI KQYRPRLGME SLLAKPISKS SAIQRAGRAG REASGKCFRL YTEKAFDTLQ
     ESDLPEILRN DVLGAVLTMK ARGVQDVLAF PLMDAPETEA LEKALLNLHY LGALNDDGCI
     TSAGEKMARL PIPPSLGAVL LAAGEPEFDC VLEVIDIISC ITSGEDIFLQ VQSEEAQEEI
     EFFRKEVQRR EGDLITYLTT MQRYCSENAN RFEWCKQKKI NMRNMKQALN IRRQLRGICL
     KERLLSELPL PDPQPFTPLN PERAEAVLRC FLRGYALKTA MLAPDASYIT VHGKHVVAIH
     PASVLHGQKK EAIMFLDHVY TNKNYAKKVS AIRATWIEEA LQR
//
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