ID A0A1V6RLB7_9EURO Unreviewed; 928 AA.
AC A0A1V6RLB7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PENSOL_c002G03334 {ECO:0000313|EMBL:OQE02244.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQE02244.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE02244.1}.
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DR EMBL; MDYO01000002; OQE02244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RLB7; -.
DR STRING; 60172.A0A1V6RLB7; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000191612; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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:UP000191612}.
FT DOMAIN 201..364
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 386..561
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 103710 MW; 917D1229AD1884A1 CRC64;
MSRNDMGPPA KRHKGFGHLP AGLRDAKRKD IDNWETNRML TSGVAQRRDH EGDFMPEDEE
ATRVHLLVHD LRPPFLDGRT IFTKQLEPIS AVRDPQSDMA VFSRKGSRVV NERRQQRERQ
KQAQEATNIA GTALGNFMGI KEDEGDSAVA EPIEEAYQGG GNKFAKHMKK SGSGASAFSS
SKTMREQREY LPAFAVREDL MRVIRDNQVV VVVGETGSGK TTQLTQFLHE EGYSKFGMIG
CTQPRRVAAM SVAKRVSEEM DVDLGALVGY AIRFEDCTSD ETVIKYMTDG VLLRESLTQK
DLDKYSCIIM DEAHERALNT DVLMGLLKKV LTRRRDLKLI VTSATMNSER FARFFGGAAE
FIIPGRTFPV DLHFSRTPCE DYVDSAVKQV LAIHVSQGAG DILVFMTGQE DIEATCELVE
DRLKQLNDPP KLSVLPIYSQ MPAEQQAKIF EKAAPGVRKV IVATNIAETS LTVDGIMFVV
DAGYSKLKVY NPRMGMDGLQ VTPISQANAN QRSGRAGRTG PGKAYRLYTE TAYKNELYIQ
TIPEIQRTSL SNTILLLKSL GVKDLLDFDF MDPPPQETIS TSLFELWALG ALDNLGDLTP
LGRRMTPFPM DPPLAKLIIM AADEYECSEE MLSIVAMLSV PNVFYRPKER EEESDSAREK
FFVPESDHLT LLHVYTQWKT NGHSDAWCTK HFLHSKTLRR AKEVRDQLLD IMNKQKMPLI
SCGTDWDTIR KCICSGFFHQ AARVKGIGEF INLRTSVTMA LHPTSALYGI GHVPEYVVYH
ELLLTSKEYM STVTSVDPHW LAELGGVFYS VKEKGYSQRN RRVTEIEFNK RMEIEEQMAA
DRERAAAEKL REQERNDPIR RRMEIEVGGK SAVRKPIVKP GSKVGGLTAS SSSSRPGASG
DGAQGGGSRP GSSVVKRPTV PRRPGRAF
//
