ID A0A094DR23_9PEZI Unreviewed; 1003 AA.
AC A0A094DR23;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE Flags: Fragment;
GN ORFNames=V496_04826 {ECO:0000313|EMBL:KFY61875.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY61875.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY61875.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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:KFY61875.1}.
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DR EMBL; JPJY01000819; KFY61875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DR23; -.
DR STRING; 1420909.A0A094DR23; -.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000029302; 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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302}.
FT DOMAIN 334..497
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 519..694
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 71..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1003
FT /evidence="ECO:0000313|EMBL:KFY61875.1"
SQ SEQUENCE 1003 AA; 112797 MW; 6A2B5AB98FBF9730 CRC64;
MTLVLSNLSA DLFCSWSVQV SFHRWWWRPV YFDVGPGGFT LVKATPRATP RATQDSTAPF
LTFLGYRFGT SSRASTPRGQ SQYPSTPRQH EFDGPEPSVA VEDSNALDRD WYGGDEGGHV
FGDEMHNPFG SYDTSWEERQ REAALVEKKT AKRVTARAAQ KQRDVDAWET NRMLTSGVAQ
RRDFGDDFED DEEQTRVHLL IHDLRPPFLD GRTVFTKQVD PVPAIRDNQS DMAVFSRKGS
RVVKERRQQK ERQKQAQEAT NMAGTALGNL MGVKEDEGDS AAPAPGEEGG GKGDSKFAEH
MAKKSEGASN FSQSKTLREQ REYLPAFAVR EDLLRVIRDN QVVIVVGETG SGKTTQLTQF
LHEDGYGKLG MIGCTQPRRV AAMSVAKRVS EEMECKLGST VGYAIRFEDC TSKETVIKYM
TDGVLLRESL NEPDLDRYSC VIMDEAHERA LNTDVLMGLF KKVLARRRDL KLIVTSATMN
SKRFSDFYGG APEFFIPGRT FPVDVMFHRS PVEDYVDQAV QQVLAIHVSM GPGDILVFMT
GQEDIECTCE LIQERLNALN DPPKLSILPI YSQMPADLQA KIFDRAAPGV RKVIVATNIA
ETSLTVDGIM YVVDAGYSKL KVYNPRMGMD TLQITPISQA NASQRSGRAG RTGPGKAFRL
FTEAAYKDEL YIQTIPEIQR TNLSNTVLLL KSLGVKDLLD FDFMDPPPQD TITTSLFDLW
ALGALNNIGD LTDVGLKMTP FPMDPSLAKL LITSEEYGCS EEMLTIVSML SVPSIFYRPK
ERQEESDAAR EKFFVPESDH LTYLHVYSQW KSNGYSDAWC TRHFLHPKSL RRAKEIREQI
GDIMKMQKMA MVSCGTDWDV IRKCICSGYY HQAAKVKGIG EYVNLRTSVA IQLHPTSALY
GLGYLPDYVV YHELILTSKE YMSTVTSVDP KWLAELGGVF YSVKEKGYSA REKRVTEVEF
NRKMEIETQM AEDKKNEEAR LEREKGRGEA QKEGVVVKKV AQR
//
