ID N1PWK4_DOTSN Unreviewed; 1212 AA.
AC N1PWK4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=DOTSEDRAFT_166379 {ECO:0000313|EMBL:EME47373.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME47373.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME47373.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB446536; EME47373.1; -; Genomic_DNA.
DR AlphaFoldDB; N1PWK4; -.
DR STRING; 675120.N1PWK4; -.
DR EnsemblFungi; EME47373; EME47373; DOTSEDRAFT_166379.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_001832_0_4_1; -.
DR OMA; FCYLDDK; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
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 GO; GO:0003724; F:RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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:UP000016933}.
FT DOMAIN 366..540
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 563..805
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 119..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 135364 MW; 4EA5E563BB43E4D9 CRC64;
MPKFVPRERK HRKLARQKSA FSQQDGPANA ETVVPLSQSE REEKRRKLEA ELKAQQPESK
ISGKKRKRLD KYIDTKLKKE ENLELLKKLA AQKVDTSLLQ SAKKLGRVQE TKRERFSRAL
REEKAGIDAH VTEQKPERED DATDAPHALE PAYSSPAAVE PVEPILPTVS FGAGLKRPLE
VDESGRPVIK KRRRQKKAVV EMTPSESEDE EPEDDALDAW SGFSDSDEEA RAESDVESQS
SSTPIDDSDP PGEAGSDSDD PREILEHFDG ENKPARVSAF KAWADSQRNQ ALDFTPSTAP
PSDDVIKANF KPRALSPDPT ISEVLATVKQ SENSYRPEKA VVIPRSEEIQ AARLQLPVVQ
EEQKIIEAVH NNVVTVVCGA TGSGKTTQIP QMLVENGYTS KGMIGVTQPR RVAAQSVARR
VAHEFGPEFG KQVGSQIRYD SNVGRNTKVK FMTDGILLRE IGQDFALSKY SVVVVDEAHE
RSVNTDILIG MLSRIVPIRE TLSKEQPEKY HPLKLVIMSA TLRVTDFMMN EKLFKTVKPP
VVEAEGRQYP VTEHFAKKTQ RDYVTETVRK VSRGHRKLPA GSILVFLTGQ DEISTVARKL
REALTNSEDA SFVNSRKPFR ITEDKPVNDY LEGEDRPADD SEDEAEIIEV DEDADDELFE
VDPDPDAPQQ TGGLKPHIVP LYGGLSSEQQ MRVFDPPPEG HRMIVLATNI AETSLTIPDV
RYVFDCGRSK EKHYDIATGV QEFRIDWISK ASASQRMGRA GRTGPGHCYR LYSSAIYEQY
FDKHTLPEIL RTPIEGTVLS LKDMEVNNVV NFPFPTPPQR EQLAQAERLL NNLGAIHPKS
GKITARGREL QRYPVNPRFG RMLELGLQHG VLAYTIALVA GLAVGELFIP ETQVVPRQEA
LADDDGDSAN EGRPKRIDRV MERAINSKKQ AFGRAHATFA NFDDKSDAIK LLTAIAAHAD
ADARGDKSFC SQYFLREKGM TEVQQLRSQL DNIMQKQMIE RGQYPEPYQA VIAPPNEKDI
KMLNQIVTAG YIDQVAVRND LLPTATSTSQ KARRAIEVPY RTLLPSVAEA DIDRVSDLEE
QAQQRSVYVH PSSLLAKLSV HEMPDYIVYT NLSRAAASTV DGKQKRIRMH PLTTAGPKLL
SSLAEGSPLL EFGKPVGKIE EQDAGRKRVC FVSTSLRDPA TPGAMPWPMK AWRVQQVRKG
KEWTVEKVLH RG
//
