ID A0A319CF36_9EURO Unreviewed; 1198 AA.
AC A0A319CF36;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=BO82DRAFT_65619 {ECO:0000313|EMBL:PYH82321.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH82321.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH82321.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH82321.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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; KZ821696; PYH82321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CF36; -.
DR STRING; 1448315.A0A319CF36; -.
DR VEuPathDB; FungiDB:BO82DRAFT_65619; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000248340; 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:PYH82321.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340}.
FT DOMAIN 367..544
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 567..812
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 83..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 133418 MW; F98CFDE40CB46DE9 CRC64;
MPKFVPRQRK QKHRQQAEST AGVDTNAAEI LPVSKSEKEA KRQKLKEELK SQNPTISSKK
QKRLDKYIET KLKKEENIEL LKKLAQSKVD TSALQSTKEL GKRKRPDERP PRPTTTDRNA
SHVDYSSGDE TDDSLPPAKS IAIASTPAES QTVGSGLKRP LEIGPDGFPI LKKRKRAPKK
KPMITISMPE VPWDGFGSDD EGEKEEDEEE VDKEHSGEDS DETSEDDKSE DDSDSGSDED
EDEDGESNDD EEEDDEDDED EEEDMGDLKK IKPRQSAFKD WARQQINEAV GFTPTTVPIV
AEPMPFIPES KRPVRNTVYV EEPLPRELQV TTGDPNRKAF SVQVNRSEEI QQARLGLPVV
GEEQKIMEAI YNNPSIVIWG ATGSGKTTQL PQFLFEAGYG HPDGPNPGII AVTQPRRVAA
VSMAKRVGDE LGQFSDRVSY QIRFDSTATS KTAVKFMTDG ILIREIAEDF SLKKYSVIVI
DEAHERSVNT DILIGMVSRI VDLRKSMSEE DPSVKPLKLV IMSATLRISD FTQNPSLFRQ
GPPPLVQAEG RQYPVTIHFS RRTHRDYIEE SFRKVSRGHR KLPPGGILVF LTGQNEIRQL
SKRLKQTFKP TQRADTTQVK VQISANDAPL ETEDLEIGGA DLSVPGGEGD DESDYEITGL
DEPDEEDEEF DLGEEAMSST TRVHVLPLYS QLPTKEQLKI FEEPPEGSRL IVLATNVAET
SLTIPGIKYV FDCGRAKEKQ YDLSTGVQKF QIEWISKASA NQRAGRAGRT GPGHCYRLYS
SAIYENEFAE YTDPEILRTP IEGVVLQMKS MGLHNVINFP FPTPPSRQGL AKAEKLLKNL
GALTSEGKIT QIGTRLSTYP LSPRFGKMLY VGHQHGCMPY VIALVAALAV GDLFVPQSQI
DPVSSKSNDD GGVYTNADRL EDTAREQRHK DYARAHRLFS KHDDTSDAMK YLSAICAYGY
ASDGDSFCEK MFLRAKAFKE ATQLRRQLTD IVRTNNPGLV GAYQARLPEP SEKQVKALKQ
IITAGFIDNV ALRADLAPVP PEMARTPKRA IDVPYFTLMR SREGPGLELN EKCVYVHPSS
ILAQMSAKEM PQYIVYSHLQ QSSPSVVAAE QTPKIRMYPL ATPSGLQLSA IAHNTPLIEY
GKPIGKAETI EGIPERRSCW VIPALVGEAG GSRWPLPAKK VIQKKDPKEG WVIEKFVS
//
