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Database: UniProt
Entry: A0A1I7RNS8_BURXY
LinkDB: A0A1I7RNS8_BURXY
Original site: A0A1I7RNS8_BURXY 
ID   A0A1I7RNS8_BURXY        Unreviewed;      1182 AA.
AC   A0A1I7RNS8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=BXYJ_LOCUS12289 {ECO:0000313|EMBL:CAD5232198.1};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0236500.1};
RN   [1] {ECO:0000313|WBParaSite:BXY_0236500.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:CAD5232198.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5232198.1};
RA   Kikuchi T.;
RL   Submitted (SEP-2020) 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};
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DR   EMBL; CAJFDI010000005; CAD5232198.1; -; Genomic_DNA.
DR   EMBL; CAJFCV020000005; CAG9124262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7RNS8; -.
DR   SMR; A0A1I7RNS8; -.
DR   WBParaSite; BXY_0236500.1; BXY_0236500.1; BXY_0236500.
DR   eggNOG; KOG0922; Eukaryota.
DR   Proteomes; UP000095284; Unplaced.
DR   Proteomes; UP000582659; Unassembled WGS sequence.
DR   Proteomes; UP000659654; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd21691; GH2-like_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR   PROSITE; PS50126; S1; 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:UP000659654}.
FT   DOMAIN          221..291
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          532..695
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          713..893
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..188
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1182 AA;  134685 MW;  73EE55997940666A CRC64;
     MDDLERLEHL SLVSKIVTEL ENHFDINDKE VAEFVISLAK ENPTFDKFKN ALIQFELDQF
     DDNLIQHLLR LVVTMEPKKV TKKKRTPSPE VEHKEDGDHF IKTIADEKEV LKKKLPALAM
     PNEPQPTSES LLGELEQLYQ KDLQAKQRNR SRSRSPHGRK RRSRSRDRDR RRRSRSPDGS
     RRRRSRSRDR GRSDRDRDGR RRRSRSPRDR KPQLLDEVEV GKIYEGRVNN IQSFGAFIVL
     DGFRKKTEGL CHISQLRNGA RVKEVTEVVN RGDRVKVKVL KTGDKISLSL KEVDQRTGED
     LNPVDAPLSE DAIGVADRRP DAPWMNPERE TAEQTSVAAP GTSSRSRVRL STPERWELQQ
     MKGGGAISLM DYPDFDEEKG ILNNPDESDG EDLEIELVED EPAFLKGYGK HVQEIEAVKV
     VKNPDGSLAQ AALMQSALSK ERRDMKTQQQ REKEGQKPRG GVSGNKILDP MAPNETRYEE
     DEPAPPSRGR EMPEWMKHVT AGGTATYGKR TSLTMKEQRE SLPIFQLKTA LLQAIHDNQI
     LVVIGETGSG KTTQMTQYLV EAGYASRGRI GCTQPRRVAA MSVAKRVSEE FGVRLGQEVG
     YTIRFEDCTC SDTIIKYMTD GMLLRECLLD PDLMSYSCIM LDEAHERTIH TDVLFGLLKA
     AVKKRPELKL IVTSATLEME KFSEYFFGAP TFTIPGRTFP VEILYTKEPE TDYLDAALIT
     VMQIHLTEPP GDILVFLTGQ EEIDTACEIL FERMKKLGSE VPDLIILPVY GALPSEMQTR
     IFEPAPPGSR KVVIATNIAE TSLTIDGIYY VVDPGFVKQK IYNPKSGMDS LVVTPISQAA
     AKQRCGRAGR TGPGKCYRLY TERAFRDEML PSPIPEIQRT NLASTLLQLK AMGINNLLEF
     DFMDAPPAEA MITALAQLYD LSALDDDGLL TKLGRRMAEF PLEPSLSKLL IMSVDLSCSD
     EVLTIVSMLS VQNVFYRPKE KQELADEKKS KFHQPEGDHC TLLAVYNSWK HHHFSQSWCF
     ESFIQVRTLK RAQDVRKQLL TIMDRHKLNI ISCGRDVQRV QKAICSGFFR NAAKRDPQEG
     YRTLVDGQTV YIHPSSSLFQ NQPEWVVYHE LVMTTKEYMR EVTLIDPRWL IEFAPSFFKF
     ADNTKLSAYK KNQRIDPLHN KYEDPNAWRL SRLKKKIYNP NR
//
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