ID A0A1S3WMG7_ERIEU Unreviewed; 1215 AA.
AC A0A1S3WMG7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DHX8 {ECO:0000313|RefSeq:XP_016047482.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016047482.1};
RN [1] {ECO:0000313|RefSeq:XP_016047482.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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}.
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DR RefSeq; XP_016047482.1; XM_016191996.1.
DR AlphaFoldDB; A0A1S3WMG7; -.
DR STRING; 9365.ENSEEUP00000004449; -.
DR CTD; 1659; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000079721; 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 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 Helicase {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|RefSeq:XP_016047482.1};
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:UP000079721}.
FT DOMAIN 260..331
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 570..733
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 751..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 138582 MW; 69F1662EC15C2356 CRC64;
MAVAVALGAS VIGTELGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA EFVISLAEKN
TTFDTFKASL MKNGAEFTDS LISNLLRLIQ TMRPPAKPST SKDPVVKPKT EKEKLKELFP
VLCQPDNPSV RTMLDEDDVK VAVDVLKELE ALMPSAAGQE KQRDTEHRTK KKKRSRSRDR
GRDRERDHNR DHKRRRHRSR SRSHSRTRER NKGKSRYRSR SRSQSPPKDR KDRDKYGERN
VDRWRDKHVD RPPPEEPAIG DIYNGKVTSI MQFGCFVQLE GLRKRWEGLV HISELRREGR
VANVADVVSK GQRVKVKVLS FTGTKTSLSM KDVDQETGED LNPNRRRNLI GETNEETSMR
NPDRPTHLSL VSAPEVEDDS LERKRLTRIS DPEKWEIKQM IAANVLSKEE FPDFDEETGI
LPKVDDEEDE DLEIELVEEE PPFLRGHTKQ SMDMSPIKIV KNPDGSLSQA AMMQSALAKE
RRELKQAQRE AEMDSIPMGL NKHWVDPLPD AEGRQIAANM RGIGMMPNDI PEWKKHAFGG
NKASYGKKTQ MSIIEQRESL PIYKLKEQLV QAVHDNQILI VIGETGSGKT TQITQYLAEA
GYTSRGKIGC TQPRRVAAMS VAKRVSEEFG CCLGQEVGYT IRFEDCTSPE TVIKYMTDGM
LLRECLIDPD LTQYAIIMLD EAHERTIHTD VLFGLLKKTV QKRQDMKLIV TSATLDAVKF
SQYFYEAPIF TIPGRTYPVE ILYTKEPETD YLDASLITVM QIHLTEPPGD ILVFLTGQEE
IDTACEILYE RMKSLGPDVP ELIILPVYSA LPSEMQTRIF DPAPPGSRKV VIATNIAETS
LTIDGIYYVV DPGFVKQKVY NSKTGIDQLV VTPISQAQAK QRAGRAGRTG PGKCYRLYTE
RAYRDEMLTT NVPEIQRTNL ASTVLSLKAM GINDLLSFDF MDAPPMETLI TAMEQLYTLG
ALDDEGLLTR LGRRMAEFPL EPMLCKMLIM SVHLGCSEEM LTIVSMLSVQ NVFYRPKDKQ
ALADQKKAKF HQTEGDHLTL LAVYNSWKNN KFSNPWCYEN FIQARSLRRA QDIRKQMLGI
MDRHKLDVVS CGKCTVRVQK AICSGFFRNA AKKDPQEGYR TLIDQQVVYI HPSSALFNRQ
PEWVVYHELV LTTKEYMREV TTIDPRWLVE FAPAFFKVSD PTKLSKQKKQ QRLEPLYNRY
EEPNAWRISR AFRRR
//