ID A0A074ZDY7_9TREM Unreviewed; 1618 AA.
AC A0A074ZDY7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KER25388.1};
GN ORFNames=T265_14212 {ECO:0000313|EMBL:KER25388.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER25388.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER25388.1, 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};
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DR EMBL; KL596778; KER25388.1; -; Genomic_DNA.
DR RefSeq; XP_009170861.1; XM_009172597.1.
DR STRING; 6198.A0A074ZDY7; -.
DR GeneID; 20328378; -.
DR KEGG; ovi:T265_14212; -.
DR CTD; 20328378; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000054324; 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; 1.10.10.2130; DEAH helicase family, winged-helix domain; 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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR042035; DEAH_win-hel_dom.
DR InterPro; IPR049588; DHX8_GH2-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF13414; TPR_11; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 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.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054324};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 104..137
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 138..171
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 556..627
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 894..1057
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1120..1300
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 259..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 786..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 264..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 182060 MW; 95BA1A01120753F7 CRC64;
MLERRSILRL SDTASEFALF GGHFTITCLV GHHFEVLGLA ELAHREYQAG EYERAEQHCM
QLWNQDPENT STLLLLSSIH FQCRRMERSA YFSQLAIKQN PLMAEAYSNL GNVFKERGQL
KEAIDNYRHA LSIKPDFIDG YINLAAALVA AGDMESAVNA YATALQYNPD LYCVRSDLGN
LLKALGRLDE AKILERDGSI QKAEPMIRLV SEDRPLDARK LGYSGSGVEV RNRLPLGTNS
VDPKLMAKPI VVITPCAPES RPTKSAASPD SSFHSTTTDL SLTKGSDDLE EVVRSTISHD
ELPAFISEAS AGIEKLEDDA FRRLEYFSLV SKVCTELTNH LGLDDKSLAE FVIHLARKNQ
TFDKFKAALV KKGAEFTDPL IASILRLVQK MLPQKTSKQK KDKKKAATAS MGAESTEPGE
RMVDEKLELR KRLLPALCIP NEDPNQMHFK HDGFEQCTTV SADQSDTSSS SFIHPDDEHL
LKEPETYAQR ERNDVDELAA SDMLKDLEQL LSGAKAESLA PRKKARSPRR RGSRSPDNRG
ASSSRRPTLP VEPVVGTIYT GRVTNILAFG AVVQLEGLRK RWEGLVHISQ IRQEGRVANV
SDVVQRMQKV YVKVLSFTGT RTSLSMKEVN QETGEDLNPR GRGKSPSGHQ TDPAKGKMRN
VDEVDIDGAR NPDRPDAGLS ASTLLFRPRK DVMEEDLDSG PKRKVQRISS PERWELKQMM
SAGVIEKTEL PDFDEETGLL PREDEESDED MEIELVEEEP PFLKGHGRHA MDLSPVRIVK
NPDGSLQQAA MMRQALQKER REMKQQERQS QMMAEREAAP ERMGKDWHDP MGASLDAKPQ
FGGPRSSEQF KDVPEWKRAV QGGTRTGAVG KKIVRSILEQ RQSLPIFKLK DELLHAVNDN
KVLIVIGETG SGKTTQITQY LAEAGFTNTG RIGCTQPRRV AAMSVAKRVS EEFGCRLGQE
VGYTIRFEDC TAPETKIKYM TDGMLLRECL IDPDLRQYSV IMLDEAHERT IHTDVLFGLL
KKAIQKRDDM KLIVTSATLD SVKFSQYFFE AASIHVNNFR TKLPGLVALR EPIFIAPAAS
QEGHLPFYRL IFLLLQPIFT IPGRTYPVEI LYSLEPENDY LDAALNTVMQ IHLTEPPGDI
LVFLTGQEEI DSGCEILYER MKALGSDVPE LIILPVYAAL PSEMQSRIFD PAPPGSRKVV
IATNIAETSL TIDGIYYVID PGFVKQKVYS SKSGMDQLIV TPISQAQAKQ RAGRAGRTGP
GKCYRLYTER AYRDEMLATN VPEIQRTNLA STVLQLKAMG INDLLSFDFM DPPPLQTLVA
AMETLHGLSA LDDEGLLTRL GRRVCLVDPR TSLSFVIAIV FRQPECFASF QMAEFPLEPM
LSKMLIMSVH LQCSEEVLTI VSMLSVQNVF YRPKEKTELA DQRKAKFHQP EGDHLTLLAV
YNAWKNNKFS APWCYDNFIQ ARTLKRAQDV RKQLLGIMDR HKLDVVSCGK KTALAQKAIL
SGFFRNAAKK DPQEGYRTLV DQQVVYIHPS SALFNRQPDW VVYHELVMTT KEYMREVTTI
DPRWLVEFAP NFFKFGDPTK LSRAKKSMRI EPLYSKFEEK DSWRISRAPR KFHVKVTF
//
