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Database: UniProt
Entry: A0A075A8U5_9TREM
LinkDB: A0A075A8U5_9TREM
Original site: A0A075A8U5_9TREM 
ID   A0A075A8U5_9TREM        Unreviewed;       765 AA.
AC   A0A075A8U5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=T265_12857 {ECO:0000313|EMBL:KER32140.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER32140.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER32140.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) 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};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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DR   EMBL; KL596637; KER32140.1; -; Genomic_DNA.
DR   RefSeq; XP_009164156.1; XM_009165892.1.
DR   AlphaFoldDB; A0A075A8U5; -.
DR   STRING; 6198.A0A075A8U5; -.
DR   GeneID; 20327025; -.
DR   KEGG; ovi:T265_12857; -.
DR   CTD; 20327025; -.
DR   OrthoDB; 5488182at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
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   CDD; cd17973; DEXHc_DHX15; 1.
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; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044756; DHX15_DEXHc.
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:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324}.
FT   DOMAIN          104..270
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          295..475
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          734..762
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  87404 MW;  E01BAD7C832F382C CRC64;
     MSSRHRIDIG ESKPRKSRRS VVHLNGERYD ELDLETFTDG PDGYSNRERS RSPERNNSKA
     HMPIPTSYSV QVNPYNGKPF SARYFDLFRK RIQLPVWEYK ENFFKVISEN QVTVLVGETG
     SGKTTQIPQW CLEWITGRYP TKKAVACTQP RRVAAMSVAQ RVSEEMDVEL GQEVGYSIRF
     EDCTSSRTVM KYMTDGMLLR EGMSDPLLEA YGVVLLDEAH ERTLATDILM GLLKEIIKQR
     LDLKIVVMSA TLDAGKFQDY FLKAPLMTVP GRTHPVEIFY TPEPERDYLE AAIRTVIQIH
     MCEEVEGDIL LFLTGQEEIE EACKRIQREV EGLGPDVGEL RCIPLYSTLP PNLQQRIFDP
     PPPKRANGAI GRKVVVSTNI AETSLTIDGV VFVIDPGFAK QKVYNPRIRV ESLLVTAISK
     ASAQQRAGRA GRTKPGKCFR LYTEKAYANE MQENTYPEIL RSNLGTVVLQ LKKLGIDDLV
     HFDFMDPPAP ETLMRALELL NYLAALDDDG NLTDLGSMMA EFPLDPQLAK MVIASCDFNC
     SNEVLSITAM LSVPQCFVRP ADAKKSADEA KMRFAHIDGD HLTMLNVYHA FKQNHEDPQW
     CYDNFVNFRS LKSADNVRVQ LSRIMDRFCL RRSSTDFSSR DYYLNIRKAL VSGFFMQVAH
     LERTGHYLTV KDNQVVQLHP STVLDHKPEW VLYNEFVLTT KNYIRTVTEV KPDWLVRIAP
     QYYDMSNFPE CEAKRLLERI VQRIQNKRLQ QEQKQAQEAK AKVSA
//
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