ID A0A401L8Q6_ASPAW Unreviewed; 1199 AA.
AC A0A401L8Q6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AAWM_10838 {ECO:0000313|EMBL:GCB27953.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB27953.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB27953.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB27953.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-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}.
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:GCB27953.1}.
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DR EMBL; BDHI01000029; GCB27953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401L8Q6; -.
DR STRING; 105351.A0A401L8Q6; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:GCB27953.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000286921}.
FT DOMAIN 366..543
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 566..811
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..123
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..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 133623 MW; E1D0B0898095BAA3 CRC64;
MPKFVPRQRK QKHKQREATT APVDTNVAEL APVSKDEKEA KRQKLKEELR AQHAQVSSKK
QKRLDKYIEN KLKKEENLEL LKKLAESKVD TSSLQSSREL GKRKRQDEVP AVSRTAEPDS
RLDQDLDLSD DDSDDSLPQL KTTVSASKSE APAQKPAENP AIGIGLKRPL ELGPDGFPVL
KKRKQVSKKP EITITMPEVP WEGFGSDEDQ DEDEKSEEGE DEDSEGTSSD GSSDEGSESD
GEEEEDDEDD DEESEEDEDE EDKEEEKHKV GQPRQSAFKS WARQQINDAI GFKPTTVPVV
EEQPFIPERK KPVRNTVAEE EPLPLELQVT TGDPNRKAFS VQVNRSEEIQ NARLGLPVVG
EEQKIMEAIY NNSSIVIWGA TGSGKTTQLP QFLFEAGYGN PDSPNPGMIG VTQPRRVAAV
SMAKRVGEEL GEFSDQVSYQ IRFESTASSK TAIKFMTDGI LIREIAEDFS LSKYSVIVID
EAHERSVNTD ILIGMVSRIV DLRKAMQEED PSVKPLKLVV MSATLRISDF TQNPNLFRQG
PPPLVQAQGR QYPVTIHFSR RTHRDYVEEA FRKVSRGHRK LPPGGMLVFM TGQNEIRQLS
KRLKQAFKPT QRGEATQAKV QISANDAPLE AEDLEIGGTD LSLAGNQEDD ESDLEITGLD
EPEEDEDEFD LGEEAMSSTT RVHVLPLYSQ LPTKEQLRVF EPPPEGSRLI VLATNVAETS
LTIPGIKYVF DCGRAKEKQY DLATGVQKFQ IEWISKASAN QRAGRAGRTG PGHCYRLYSS
AIYENEFAEY TDPEILRTPI EGVVLQMKSM GLHNVINFPF PTPPSRQGLA KAEKLLKNLG
ALTSEGQITP IGNRLSTYPL SPRFGKMLYV GHQHGCMPYV IALVSALAVG DLFVPENQID
PVPANKDDNE GKGVYTNSDR LEDTAREQRH KDYARVHRLF SKHDDTSDAL KYLSAICAYG
YASDGDSFCE KMFLRAKAFK EATQLRRQLT DIVRSNNPGL VQAYQARLPE PTEKQVKAIK
QIITAGFIDN VALRADLAPV PPEMHRTPKR AIDVPYFTLM RSRDGPGLEL DDKAVYVHPS
SVIAQLSAKE MPQYIVYSHL QQSSPSIVSA DQTPKIRMYP LATPSGLQLS ALAHGTPLIE
YGKPIGKTEL IEGIPQRRSC WVIPSLVGEA GGSRWPLPAK KVIQRKDAKE GWVIEKFVA
//