ID A0A395RQV1_9HYPO Unreviewed; 1368 AA.
AC A0A395RQV1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dead deah box helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FLONG3_10311 {ECO:0000313|EMBL:RGP62232.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP62232.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP62232.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP62232.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP62232.1}.
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DR EMBL; PXOG01000293; RGP62232.1; -; Genomic_DNA.
DR STRING; 694270.A0A395RQV1; -.
DR Proteomes; UP000266234; 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; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
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; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234}.
FT DOMAIN 592..768
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 829..994
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 151919 MW; 9F94DDD4946F5505 CRC64;
MVKKGKGKAA GGIDLSDPMP LGSSKDQIKG KKGQKGGTST PEAAPTAGPP KPTVKQLIGG
SSWTGKLPVN LLSEYCQKQR WERPDYDTRK TPEGFSVWVT MSAKDPKTQQ ITKLEPFKIP
ATHKHLIMRP TAIEAKHAAA TYALFRVCSM QNKHTVLPPE HKSLWKDFQA LKAQDVKEGK
AWMYEPDPFK ALQERQEAKA AADKKRKEIE AAKAKAAAMP GAAGLVLMSN AGKGDGRSSN
IMKGWSTAPK VEMGKKTRAQ LETLLRTGVK WNPNDVQMSK FQKEAIVAEL SKLSFRKSHV
EEAVEYCKDR EETLEWLLIH VPEDDLPRWA LPESYAAGVS VGATNLRREG IIKRLAQAGY
SLELATRVLD EQGIDEDKAA ETLQNLLFPV ESNNSDDADF LDLGTPEEQW EEEVGSLEAM
YGDGFERQGD NVIRIKLDSV KNGQQLVDTS LQIRRPVTYP ASLILTIVAN IPSYIKLSII
RKALEYIEES LRDEPMKIYL AMDWIQQNIN SIIADPGKLV DISAVSSAAA EYKPIAAIAQ
KKRPARAPKL IKWVKDEKNR EQWLRRQEST PLKNMISKRQ NLPAWQMREA IIGTVRSNHV
TIISGETGSG KSTQSMQFIL DDLYAQGLGG CANMIVTQPR RISALGLADR VAEERCSRVG
EEVGYAIRGE SKRSKDTRIT FVTTGVLLRR LQTSGGRVED VVASLADVSH VVIDEVHERS
LDTDFLLNLI REVMKSKKDM LKLILMSATL DAATFKNYFA SEGLSVGTVE IEGRTFPVDE
YYLDDVIRMT AYGVESSDTE FISGDALGRV IQKLGHRINY NLLVETVKAI DFELSYEKKS
GGILIFLPGV GEINQACRAL KAINSLHVLP LHASLETREQ KRVFSSAPPG KRKVVVATNV
AETSITIDDI VVVIDSGKVK ETSFDVQNNM RKLEETWASR AACKQRRGRA GRVQEGRCYK
LFTQNLEQQM PERPEPEIRR VPLEQLCLSV RAMGMKDVAG FLGRSPTPPD ATAIDGAMKL
LRRMGALDGD ELTAMGQQLA MLPADLRCGK LMVFGAIFGC LGDCVTIAAI LSTRSPFISP
QEKRDEAKEA RLKFYSGDGD LLTDLQAFQE WDSMMQERLP QRQVRSWCEE NFLNFQTLSD
ISNTRAQYYT ALAEIGIVAP SEASSEAHAH EVNSNGSQLL RALVAAAFTP QIARIQYPDK
KFASSMSGAV ELDPEARSIK YFNQENGRVF VHPSSTLFGS QGFSGNAAYM AYFSLISTSK
IFIRDLTRKY IPFNSPSVNR TNIQQAFNAY TLLLFSGPIE LDTLGRGLLV DGWLKLRGWA
RIGVLLARLR GMVDELIAKK VENPEMSVKD DEVITLVRRM IELDGLDA
//
