ID   A0A2L2T1C0_9HYPO        Unreviewed;      1270 AA.
AC   A0A2L2T1C0;
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=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI61223.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010140}.
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DR   EMBL; LN649230; CEI61223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2T1C0; -.
DR   STRING; 56646.A0A2L2T1C0; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000245910; Chromosome ii.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 1.20.1500.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   InterPro; IPR040801; Ski2_N.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   Pfam; PF17911; Ski2_N; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245910};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          306..462
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          592..794
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          9..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1270 AA;  141790 MW;  5084DCF7A3F751D0 CRC64;
     MAAIDALLEG EAQEIGQRQP STQDSEELKR HLEELLLSPS PEFSSEWLNR LQQRWDFEAD
     YTSLYKVAPP HTRTLTRFQR HGLEGRVTGY KNVTVPANSA TAKNSTSLSR KPANRADFVR
     GAAGFFPFAP GGLEGIEATA AFEDSVHTGG VAEPGSTGNK LERVIQLGAE GGLLEIAPGM
     SRGIDFAKKK ISVSQEDANA IKEVLEEEPE EAKVGPEGDE ISPDTATPEL NADSGEDGDD
     IDGILPVEFP ALEPHGVLAA SSARKAGREW AHMVDINHDM SNFRELVPDM AREWPFELDT
     FQKEAVYHLE NGDSVFVAAH TSAGKTVVAE YAIALAAKHM TKAIYTSPIK ALSNQKFRDF
     RQTFDEVGIL TGDVQINPEA SCLIMTTEIL RSMLYRGADI IRDVEFVIFD EVHYVNDFER
     GVVWEEVIIM LPEHVSLILL SATVPNTKEF ASWVGRTKQK DIYVISTPKR PVPLEHYLWA
     GKDIHKIVDS EKKFIEKGWK DAHFAIQGRD KQKPAEATVA ARGGNPRGNQ RGGTQRGGPQ
     RGGRGGGQQR GGNQQRGRGG PPRASHAPGH MGRGGRAGGF TSVAQDKNLW VHLVQYLKKQ
     TLLPACIFVF SKKRCEENAD ALSNQDFCTA SEKSHIHMII EKSVARLKPD DRQLPQIIRL
     RELLSRGIAV HHGGLLPIVK ELVEILFAQT LVKVLFATET FAMGLNLPTR TVVFSGYRKH
     DGHSFRNLLP GEYTQMAGRA GRRGLDTVGS VIIVPPGGLD DAPPVADLRN MILGEPSKLR
     SQFRLTYNMI LNLLRVEALK IEEMIKRSFS EHATQQLLPE HEKDVKLAQA DLAKVKRDSC
     EICDVSMDEC HQASQDFKKL TFDLYKGLLA IPIGRRMFSQ HRLVVFNWDG IRSVGILLAD
     GISNKGTSED PTLHICAIKS LRDRRDATDQ LPFVPAFRKY FHELPKSKKR VQTKTLHVPL
     SDVECLTRWV TKGIVPEIFQ GGDGYHQAKD RLQELCGSWD DRLEELDLSR IKQLQLQEIV
     ETRVDLVKTI SNSPAERCSE FLKHFAMCHD EWLIKEHISQ LKQSLSDQNL QLLPDYEQRV
     QVLKELGFID DATRIQLKGK VACEIHSGDE LVLTELILDN VLADYEPAEI AALLSAFVFQ
     EKTDMEPSLT GNLERGKETI VAISEKVNDV QTRLQVIQSA DDSNDFVSRP RFGLMEVVYE
     WARGMSFKNI TGLTDVLEGT IVRTITRLDE TCREVKNAAR IVGDPELYQK MQQAQEMIKR
     DITAVASLYM
//