ID A0A158Q7Q5_9BILA Unreviewed; 1201 AA.
AC A0A158Q7Q5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000528201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000528201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 AlphaFoldDB; A0A158Q7Q5; -.
DR STRING; 1147741.A0A158Q7Q5; -.
DR WBParaSite; EEL_0000528201-mRNA-1; EEL_0000528201-mRNA-1; EEL_0000528201.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR CDD; cd17971; DEXHc_DHX8; 1.
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; IPR044762; DHX8/Prp22_DEXHc.
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}.
FT DOMAIN 234..304
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 551..714
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 739..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 121..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 136697 MW; 7C2F703BF04CB373 CRC64;
MEELERLSLV SRVCVELDNH FGLADKDVAE FIIYLATENP TFDKFKKSIT KEGLADQFDD
SLLANLLRII QHMQLKKKDV GNAKNLSDDK ELLRETLPAL AMPNVDANKL MTELEGLQSK
WKEQKAKTTD KLDKKRNGHR SRSVDTEKRN HRHSSDDRKD RHYHDRRHRQ SSTERDRKRK
RSEGRSPVEK YRRRERSRDR SEKQDESSSR RRSRRSRSHS SESGRRISVA PVVGEIYNGR
VTSIQSFGAF VQLEGLRQRF EGLLHISQIR QDRINAVSDV LNRNQKVKVK VIKFELGKIG
LSMKEVDQET GEDLNPREPI SLVDGARPPR NPEAPWMDPS ASRNPGDVSL TQSKSVAKSR
VRLTTPERWE LRQMQGGGAI TNADLPDFDE ELGVLRNYDG VFVKESDGED IEIEIVEEEP
EFLRGYGKCM LDLEPVKVVK NPDGSLAQAA LMQSALAKER RDQKLQAQRE QESHSQRSGL
SSTARINDPM AELSVQSSVD TSGPSQRQKE MPEWLRHVTA GGKATYGKRT NMSLREQRES
LPIFALKKAL LEAVAAQNIL IVIGETGSGK TTQITQYMVE VGYTARGRIG CTQPRRVAAM
SVAKRVAEEM GCRLGSEVGY TIRFEDCTSQ DTVVKYMTDG MLLRECLLDP DLTSYSVIML
DEAHERTIHT DVLFGLLKAA VKKRPELKLI VTSATLDAVK FSEYFYEAPI FTIPGRTFPV
EILYTREPET DYLDAAHITV MQIHLTEPPG DILVFLTGQE EIDTSCEVLY ERMKSLGPDV
PELIILPVYG ALPSEMQTRI FEPAPLGSRK VVIATNIAET SLTIDGIYYV VDPGFVKQKI
YNPKSGMDSL VVTPISQAQA KQRAGRAGRT GPGKCYRLYT ERAYRDEMLP TPVPEIQRTN
LASTLLQLKA MGINNLIDFD FMDAPPVEAM ITALTQLHTL SALDNDGLLT RLGRRMAEFP
LEPSLAKLLI MSVDLCCSDE VLTIVSMLSV QNVFYRPKDK QEIADQKKAK FHQPEGDHLT
LLAVYNSWKH HHFSQPWCYE NFIQIRTLKR AQDIRKQLLS IMDRHKLNTI SCGRDVQRIQ
KAICSGFFRN AAKRDPQEGY RTIVDGQNVY IHPSSALFQN QPEWVVYHEL IMTTKEYMRE
VTAIEPKWLV EFAPSFFKMG DNTKLSAFKK NQTINPLYNK YEDPNAWRIT RLKKKIYNPN
R
//
