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Database: UniProt
Entry: A0A2K0VVB7_GIBNY
LinkDB: A0A2K0VVB7_GIBNY
Original site: A0A2K0VVB7_GIBNY 
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}.
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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
//
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