ID A0A1V6Z1U7_PENNA Unreviewed; 1123 AA.
AC A0A1V6Z1U7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PENNAL_c0005G09269 {ECO:0000313|EMBL:OQE93661.1},
GN PNAL_LOCUS10585 {ECO:0000313|EMBL:CAG8330565.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE93661.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|EMBL:OQE93661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE93661.1};
RA Nielsen J.C., Nielsen J.;
RT "Uncovering the secondary metabolism of Penicillium species provides
RT insights into the evolution of 6-MSA pathways.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
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).
RN [3] {ECO:0000313|EMBL:CAG8330565.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
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:OQE93661.1}.
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DR EMBL; CAJVNV010000641; CAG8330565.1; -; Genomic_DNA.
DR EMBL; MOOB01000005; OQE93661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Z1U7; -.
DR STRING; 60175.A0A1V6Z1U7; -.
DR OMA; HITLMNV; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000191691; Unassembled WGS sequence.
DR Proteomes; UP001153461; 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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191691}.
FT DOMAIN 485..649
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 674..847
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 96..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 127303 MW; 2DD7D4C25DE767D1 CRC64;
MDNKDFVSDN LLRLTGASEP TVVDFVLATA SSAKSTSSLQ DTLVSFLDGI NTSPAEIGAF
ARDLHVRMGK GAQPSASVSK PASKVTSQKK YRLVDMGEDQ PEPTPSLGPV NVEADRERRR
RRDRDSDRDR TSSNRDSEPR SHGEKDDSRK RDRSRDAESR DRPRTRKLRK KGSQVFEDRW
GDEEIPEDEI YPEEFEESPS KRTRLDDGSA SPLASLADDI DIDPKTKQEI ERQRDLRERD
EFAKRLANKE SSKSKKIVED RTRDGEAARR RALGDDASAR ASMMPDLRER SRQEYLKKRE
TERLALLRRQ VVEEAAELRE NPNLSRKEKE EFARNREVLR LAEERLRIDD HRDGYQMPSD
YITEKGKIDR KKKEEALYKR YVERDELGQE RFVTEHEEWE LEQAAKAKAQ IKKAEFVDEG
DYEYVFDDSQ QINFVMDAKL EGTQKPMTKE QLRFKEQVDA AEKKALSMDE TRKSLPIYQF
RDQIIQAVAD HQVLIIVGET GSGKTTQIPQ YLHEAGYTKD GLKIGCTQPR RVAAMSVAAR
VADEMGTKIG NEVGYAIRFE DNTTDKTILK YMTDGMLLRE LLTEPDLSQY SALMIDEAHE
RTVPTDIACG LLKDIAKARP DLKLLISSAT MDAQKFQKYF DDAPIFNIPG RRYPVDVHYT
SQPEANYLAA AITTVFQIHV TQGPGDILVF LTGQEEIEAA EQSLQETARK LGSKIPEMII
APIYANLPSE LQTKIFEPTP PKARKVVLAT NIAETSLTID GIVYVIDPGF VKENVFNPRT
GMESLVVTPC SRASANQRAG RAGRVGPGKC FRLYTKWAYY NELEENTTPE IQRTNLNGVI
LMLKSLGIDQ LLDFDFMDPP PAETIIRALE QLYALGALND RGELTKVGRQ MAEFPTDPML
AKAILAADKY GCVEEVLSIV SMLGEGSALF FRPKDKKIHA DSARNRFTIK DGGDHLTLLN
VWNQWVDSDF STIWAKENFL QQRSLTRARD VRDQLAKLCD RVEVAVSTCG STNIQPIQKA
ITAGFFPNAA RLQRGGDSYR TIKNGQSVYL HPSSTLMEVN PRWVIYFELV LTSKEYMRSN
MPLQPEWLVE VAPHYYKKKD LESLGLDRKV TKGQGVAGEK SRE
//
