ID G2XDY9_VERDV Unreviewed; 1191 AA.
AC G2XDY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-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=VDAG_08371 {ECO:0000313|EMBL:EGY18037.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY18037.1};
RN [1] {ECO:0000313|EMBL:EGY18037.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY18037.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; DS572714; EGY18037.1; -; Genomic_DNA.
DR RefSeq; XP_009658391.1; XM_009660096.1.
DR AlphaFoldDB; G2XDY9; -.
DR SMR; G2XDY9; -.
DR STRING; 498257.G2XDY9; -.
DR EnsemblFungi; EGY18037; EGY18037; VDAG_08371.
DR GeneID; 20709834; -.
DR KEGG; vda:VDAG_08371; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_2_1; -.
DR InParanoid; G2XDY9; -.
DR OMA; FCYLDDK; -.
DR OrthoDB; 5490433at2759; -.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 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:0000313|EMBL:EGY18037.1};
KW Helicase {ECO:0000313|EMBL:EGY18037.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000313|EMBL:EGY18037.1}.
FT DOMAIN 420..556
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 578..816
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 131939 MW; 1E0D18F1FC59D2FE CRC64;
MAKFVPRQRK HKVLAREKAK ENAVAPLDAD TNAEQIDPEE RRLMREKKER MKKELQGDVK
VSGKKAKRLD KYIENKLRKD ENREILAKLS QSKIDTNLFT SSKTIGQGKE TKRQAISRAM
RERKAGVEVD EDGDELLFER PRQQDSSSDE DSEDDEPAPA PAPIPAQKPA SPPTEAPTAI
SAPQPSAAAA GSGLKRPLDL DEAGRPVLRK RQRRGGVQSK FTIAEPAKGD LEEEWSGFSS
EDEGVGGAKL GSADTEEDAS ESGSGDDSDE DDDEEEDGES ASDEDDSDMD SDDSSSEAKP
SAFKAWAPAQ RNEALGFKPA SESTQILDVP RPDNFTPRAA EHEPLPEELQ PSVNLARKAF
GVTVTRTPEI QEARLKLPVV GEGAEDYGGH SQPRHHRRVR FHRFGKDDAS YGSPDSPTSG
MIGVTQPRRV AAVSMSKRVA EEMGDHAERV AYQIRFEGTT SAKTAIKFMT DGVLLREIAQ
DFSLKKYSAV IIDEAHERSV NTDILIGMLS RINNVRQEDQ NGSSPLKPLK IIIMSATLRV
EDMTQNSQLF ATPPPVVEVE GRQHPVTIHF ARRTRPDYVD ELYNKISRGH KKLPPGGFLV
FLTGQNEIVQ LSKRLEAAFG GLTSASGPKV QISASEAPME VEDIEFGDVD DFDAGELDDE
ISEGEGDEDE DEEFKIEEEG ETGPLKMQVL PLYSLLPTRE QMRVFKEPPE GTRQVILATN
VAETSLTIPG TRYVFDCGRS KERQYDEVSG VQTYAIGWVS KASANQRSGR AGRTGPGHCY
RLYSSAVYER DLPQFSEPEL LRMPIDGVVL QLKSMNLSNV VNFPFPTPPD RASLRKAERL
LHYLSAISAE GQVTRIGSTM SIFPLSPRFA RILLVGHQHD CLQYTIALVA ALSAAEVFIP
ENQAIPSLEA TEDHVLRTNA VVAAEDRQAT IRRAFNGVQR NFCSLDDKSD AIKLLQVVGE
YAHEPTEAWC ESHFVRYKVL KEIQQLRQQI VELLRTNVPS FQNLRFQDRL DRPTDRQVAY
LKQMVAAGFI DQVAIRADKS PTPPENARKP RRAIDVPYLP LVPLGVGADV DKFVYLHPSS
PLAHMSPQEL PEYVVYAYLQ RATQGVDPTK TPKTRMHALT DVTGGQLAGL AKGTPLLTYG
KPVKEVRATA MEREVWVVPY LRAEGVGGSG WPLPMKKVIE KREVGKGWVV Q
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