ID G7XHA8_ASPKW Unreviewed; 1202 AA.
AC G7XHA8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AKAW_04431 {ECO:0000313|EMBL:GAA86317.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA86317.1};
RN [1] {ECO:0000313|EMBL:GAA86317.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA86317.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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 ---------------------------------------------------------------------------
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; DF126455; GAA86317.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XHA8; -.
DR STRING; 1033177.G7XHA8; -.
DR VEuPathDB; FungiDB:AKAW_04431; -.
DR eggNOG; KOG0926; Eukaryota.
DR InParanoid; G7XHA8; -.
DR Proteomes; UP000006812; 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:0004386; F:helicase activity; 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 Helicase {ECO:0000313|EMBL:GAA86317.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 370..547
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 570..815
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..268
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 134131 MW; 279956B45DC0DE4A CRC64;
MPKFVPRQRK QKHKQREATT APIDTNVAEL APVSKDEKEA KRQKLKEELR AQHAQVSSKK
QKRLDKYIEN KLKKEENLEL LKKLAQSKVD TSALQSSKEL GKRKRQDEVP AVSRTADHDS
RHDQDLDFSD DDSDDSLPQS KTTVNESKSE APAQKPAENP ATGIGLKRPL ELGPDGFPVL
KKRKKVAKKP EITITMPEVP WEGFGSDEDQ DEDEESEEGE DEDSEGTSSD GSSDESGSEG
ESDEDEDEDD SEEDDEESEE DDDEEGEEEE KHKVGQPRQS AFKSWARQQI NDAIGFKPTT
VPVVEEQAFI PERKKPVRNT VAEEEPLPLE LQVTTGDPNR KAFSVQVNRS EEIQNARLGL
PVVGEEQKIM EAIYNNSSIV IWGATGSGKT TQLPQFLFEA GYGNPNSPNP GMIGVTQPRR
VAAVSMAKRV GEELGEFSDQ VSYQIRFEST ASSKTAIKFM TDGILIREIA EDFSLSKYSV
IVIDEAHERS VNTDILIGMV SRIVDLRKAM QEEDPSVKPL KLVVMSATLR ISDFTQNPNL
FRQGPPPLVQ AQGRQYPVTI HFSRRTNRDY IEEAFRKVSR GHRKLPPGGM LVFMTGQNEI
RQLSKRLKQA FKPTQRGEAT QARVQISAND APLEAEDFEI GGTDLSLAGN QEDDESDYEI
TGLDEPEEDE DEFDLGEEAM SSTTRVHVLP LYSQLPTKEQ LRVFEPPPEG SRLIVLATNV
AETSLTIPGI KYVFDCGRAK EKQYDLATGV QKFQIEWISK ASANQRAGRA GRTGPGHCYR
LYSSAIYENE FAEYTDPEIL RTPIEGVVLQ MKSMGLHNVI NFPFPTPPSR EGLAKAEKLL
KNLGALTSEG QITQIGNRLS TYPLSPRFGK MLYVGHQHGC MPYVIALVSA LAVGDLFVPE
NQIDPTPAKD DNERNGVYTN ADRLEDTARE QRHKDYARVH RLFSKHDDTS DALKYLSAIC
AYGYASDGDA FCEKMFLRAK AFKEATQLRR QLTDIVRSNN PGLVQAYQAR LPEPTEKQVK
AIKQIITAGF IDNVALRADL APVPPEMHRT PKRAIDVPYF TLMRSRDGPG LELDEKVVYV
HPSSVIAQLS AKEMPQYIVY SHLQQSSPSI VSADQTPKIR MYPLATPSGL QLSALAHGTP
LIEYGKPIGK TELIEGIPQR RSCWVIPSLV GEAGGARWPL PAKKVIQRKD AKEGWVIEKF
VA
//
