ID A0A2K0VVB7_GIBNY Unreviewed; 1209 AA.
AC A0A2K0VVB7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=FNYG_12724 {ECO:0000313|EMBL:PNP73975.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP73975.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP73975.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP73975.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) 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}.
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:PNP73975.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MTQA01000226; PNP73975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0VVB7; -.
DR STRING; 42673.A0A2K0VVB7; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000236664; 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; cd17982; DEXHc_DHX37; 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; 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; 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; 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:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000236664}.
FT DOMAIN 391..568
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 590..827
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1209 AA; 135151 MW; 3A8DB4349E1C66A7 CRC64;
MAKYVPRQRK HKVLARERAK ENAQHEVQDN PNQEILLPTA KADREARKAQ MKAELRQEGA
KMSGKKAKRL EKYIEGKLRK DESRELMAKL AEQQIDTTLF SSSRVLGQGR ETKKEALRRA
MREEKAGLEG GEEGRSEILL EKRKELNADE EISSDESEES EPDEQKPSKP TPTPAPAPTS
RESDQPKTET SAPTIGSGLK RPLEVDDEGR PVIKKRQKRG GVKSKFSLAP VETPLELESE
EADSVASDGD SDEWNGFSDD SADKDNTADD DSESDEEEYD ESSEEPEESD EDMEDADENK
AQRSSSFKAW AHQQRNEALG YQSIEGTTTN LEIPKPENFV PRAPEQDPLP MELQPTQNIN
RKVYSVTVTR IPEVQEARLK LPVVSEEQRI MEAIHNYDIV VVCGSTGSGK TTQIPQFLYE
SGYGSPDSPT PGMIGITQPR RVAAVSMSKR VGEELGDKSE VVAYQIRFEG TVDPKTAIKF
MTDGVLLREV AQDITLKKYS AIVIDEAHER SVNTDILIGM LSRVIKLRAE LAAEDPTVKP
LKLIIMSATL RIEDLTMNPT LFATPPPVLE VEGRQHPVTI HFSRRTQHDY VEEAFRKISR
GHKKLPPGDI LVFLTGRNEI LELSKKLKAT FGGPKTADGP KVQISASEAP IEVEDIEFGD
VDDRNGDDFD EIPTDDEDED DEDEFQIEED QEVAPLKMRV LPLYSLLPTR EQMRVFEPAP
EGTRNIILAT NVAETSLTIP GIRYVFDCGR SKERQYDRLS GVQSYDIGWI SKASANQRSG
RAGRTGPGHC YRLYSSAVYE RDFPPFTDPE LLRMPIEGIV LQLKAMNLQH VVNFPFPTPP
DRRALAKSEK LLTYLSAISS TGQVTQIGQT MSVFPLSPRF ARILLVGHLH DCIHYTIALV
AGLSAAEIFL PENQAIPALA AKDDTAIRTT SDVIAEDRQA NVRKMFNEVH KNFCYLDDKS
DAIKLLQVVG EFAHEPTEEW CESHFVRYKV LKEIQQLRRQ ITELLRTNVS AFTNLKYQDK
LDPPSPKQVA ALKQMVAAGF VDQVAIRADL TPNPPEQFRK PRRSIDVPYI PLIPIHAGKE
VESDCAVYIH PTSPLAHISI QECPEYIVYS YLQRATQSVD AEKRPKTRMH ALTDVTGGQL
AGLAKGTPLI TYGKPIKELK PTTGTDGATV RECFVVPYLR AESTGGQGWP LPAKKVKQRK
VPGKGWVVE
//