ID A0A443SBT1_9ACAR Unreviewed; 1165 AA.
AC A0A443SBT1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=B4U80_01428 {ECO:0000313|EMBL:RWS25016.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS25016.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS25016.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS25016.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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 -!- 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:RWS25016.1}.
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DR EMBL; NCKV01004155; RWS25016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443SBT1; -.
DR STRING; 299467.A0A443SBT1; -.
DR EnsemblMetazoa; LDEU007024-RA; LDEU007024-PA; LDEU007024.
DR VEuPathDB; VectorBase:LDEU007024; -.
DR Proteomes; UP000288716; 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: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 Helicase {ECO:0000313|EMBL:RWS25016.1};
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:UP000288716}.
FT DOMAIN 218..289
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 529..692
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 700..880
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 147..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 132432 MW; F33BC8E6FB334E87 CRC64;
MEEIKKLEYL SLVSKICTEL ENHLQINDKD LAEYIISLAD ENDTFDKFKN ALVSNGAEFT
DSFIANLLRI IQHMKPKESK TDKLDSSDDK PVDDVSMKRA LFPYLAMPND PSVRNMLDAE
LKDNKDVEVA NSAMALLEAL APKGKLEESI KRQRDDDDYS RERKYRRRSR SKSRDRHHKS
RNRSRSRERK HRRRSVSHDR NRRRREKERE LPSEPAAGMI LEGKVTNIMQ FGCFVQLEGL
KKRWEGLVHI SQLRREGRVA NVSDVVSRGQ RIKVKVLSFA GQKTSLSLKD VDQETGEDLN
PSYCRGADRL ESDDSVVRNP DRPAVLPLHL QKPTDEDVEN RRRVVQRISS PEKWELTQMV
HANVIDKSSL PDFDEATGLL PKPEESDDED IEIEIVEDEP FFLRGHGRSN AMDLSPVRIV
KNPDGSLAQA AMMQSALAKE RREQKQQQRE AEASGVPASL NMSWIDPMSE GDRGLAANIK
NTVSAPQEIP EWKKHISGGS KASYGKKTQM SILEQRQSLP IYKLKVELVR AVDDNQILIV
IGETGSGKTT QMTQYLAENG FTSTGKIGCT QPRRVAAMSV AKRVAEEFGC RLGQEVGYTI
RFEDCTSPET AIKYMTDGML LRECLIDPDL KSYSVIMLDE AHERTIHTDV LFGLLKAAVK
KRPNLKLIVT SATLDAPIFT IPGRSFPVEI FYSKEPETDY LDASLITVMQ IHLREPPGDI
LLFLTGQEEI DSACEVLYER MKSLGPEVPE LIILPVYSAL PSEMQTRIFE PAPPGSRKVV
IATNIAETSL TIDGIYYVVD PGFVKQNVYN PKTGMDQLVV TPISQAQAKQ RAGRAGRTGP
GKTYRLYTER AYRDEMLTTP VPEIQRTNLA MTVLQLKAMG INDLLSFDFM DAPPLETLLM
ALEQLHSLSA LDDEGLLTRL GRRMAEFPLE PMLAKMLIMS VHLGCSDEIL TIVSMLSVQN
VFYRPKDKQA VADAKKAKFN QSEGDHLTLL AVYNSWKNNK FSNAWCYENF VQIRTLKRAQ
DVRKQLLGIM DRHKLDVVSC GRNTARVQKA ICSGFFRNAA KKDPQEGYRT LVDGQVVYIH
PSSALFHKQP EWVVYHELVL TTKEYMREVT AIDPKWLVEF APSFFKFADP TKLSKHKKQL
RLEPLYNKYE EPNAWRISRV RRRRN
//
