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Database: UniProt
Entry: A0A401L8Q6_ASPAW
LinkDB: A0A401L8Q6_ASPAW
Original site: A0A401L8Q6_ASPAW 
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
//
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