ID A0A3M2SYY7_9EURO Unreviewed; 1190 AA.
AC A0A3M2SYY7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=PHISP_06323 {ECO:0000313|EMBL:RMJ22801.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ22801.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ22801.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ22801.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-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:RMJ22801.1}.
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DR EMBL; RAQS01000298; RMJ22801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2SYY7; -.
DR STRING; 1960876.A0A3M2SYY7; -.
DR Proteomes; UP000272442; 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; 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 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:UP000272442}.
FT DOMAIN 362..539
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 562..806
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 131559 MW; 047A6AD09E7A845D CRC64;
MPKFIPRQRK QKHRQREGAG TPAVDTNFAE VPASARNDKE ARRQDLREEL RSQHPKVSSK
KQKRLDKYID NKLKKEENLE LLKKLAQAKV DTTSLQSAKE IGKGPQDQQK PSASSEATNE
ATSHSADLSG DETDEDDLKL KTAGNENEAE TADKSTVEPP STGSGLKRPL DLGADGFPVL
KKRKRTRKAK PEPEPELPWD GFDSEDEAQS GSQNGDNLSD AEDDDEQDAS EDENSDGSSE
GTSVDEDEEE SSDEGEDSEP ARKIQPRQSA FKAWAQQQIN DAMDFKPTTG PVVPEASEEQ
PFAPPRKPAR NTVDTEEPLP LELQVTQGNP DRKAFSVQVD RAEEVQNARL GLPVVGEEQK
IMEAIHNNPA VVIWGATGSG KTTQLPQFLF EAGYGSADSP NPGMIAVTQP RRVAAVSMAS
RVADELGQFS NRVAYQIRFE SSVSRDTAVK FMTDGILLRE IANDFSLSKY SIIVIDEAHE
RSVNTDILIG MVSRIVNLRK DMNREDPSVK PLKLVVMSAT LRISDFMQNP SLFRQGPPPL
VQAEGRQYPV TVHFSKRTHR DYVEEAFRKV SRGHRKLPQG GMLVFLTGQN EIRYLSKRLK
QAFKPTQREG FQGKTQISAN DAPLEAEDLD LGVDLSKPGN AEDGDEDSDV EIMGLDNDDD
DEGFDIGEEA MDSSSRVHVL PLYSQLPTKE QLKIFESPPE GSRLIVLATN VAETSLTIPG
IRYVFDCGRA KEKQYDLFTG VQSFQVDWIS KASASQRAGR AGRTGPGHCY RLYSSAVYEG
QFSEYTDPEV LRTPIEGVVL QMKSMGLHNV INFPFPTPPS RDGLAKAEKL LKNLGALSSD
SQVTQIGRRL STYPLSPRFG KMLYIGHQHG CMPYVVALVA ALAVGDLFVP ENQIEPTSSS
EGKEDGVYTN SDRLADTAQE QRHKNYARVH RLLGKHDDTS DALKYLSSIC AYGYASDGDS
FCEQMFLRAK AFKEAAQLRS QLTDIVRVNN PGLIGAYEPR LPEPSDKQLK ALKQIVTAGF
IDNAAIRADL APEPPEMPRS PKRAIDVPYL TLFRSREGRA AELQEKAVYV HPSSMLARLS
PREMPQYIVY SHLQQASPSA ISEQVPKIRM FPLVAPSGLQ LSAIAHGTPL LEYGKPIGKV
ELLESIPQRR ACWVVPSLVG EAGSLGWPLP AKKVVQRKDA REGWVIEKLV
//
