ID A0A068YE60_ECHMU Unreviewed; 1051 AA.
AC A0A068YE60;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5 {ECO:0000256|ARBA:ARBA00041162};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5 {ECO:0000256|ARBA:ARBA00040918};
GN ORFNames=EmuJ_001058000 {ECO:0000313|EMBL:CDS42861.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS42861.1};
RN [1] {ECO:0000313|EMBL:CDS42861.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS42861.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase involved spliceosome assembly and
CC in nuclear splicing. Catalyzes an ATP-dependent conformational change
CC of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP
CC association with intron RNA. {ECO:0000256|ARBA:ARBA00037330}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000256|ARBA:ARBA00038511}.
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DR EMBL; LN902842; CDS42861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YE60; -.
DR STRING; 6211.A0A068YE60; -.
DR eggNOG; KOG0334; Eukaryota.
DR OMA; HSIRKRF; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd22473; KH-I_DDX46; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47958:SF35; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CDS42861.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 362..390
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 393..571
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 599..744
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..390
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 13..47
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 115874 MW; 11BF2D7D251ABFFC CRC64;
MFASVMGRHD RSPYRSSRRH RSRSSSRHRH HRRHRRDRSR SRSPRDYRHH RNSVLASSSS
SSLGSLLAAN SSQKDGTPSR SERVSSVALE ALSKIKAAQN RGADESGSGV SGLEGALIID
STLDKDAEQK RLELEMQKRR ERVERERREK RLKQDVVTAH SKLLDGIKMR SLKKWSLEDD
DDDDVPPPTV IKEDTLVKEE EDEVDPLDAY MQEVSKEAHQ QVDDTTVLHL VQTPAGLIQA
PGLVTNPQLG PGNNVTTKDS QKTQKKVGRG ELVLDEDEQD VDMPYYPEPE ERISIADALA
QLQKREKLGA VDHSKIDYQP FTKDFYVEVP EIAKMTKEQV KVYRQQLENI HVRGKDCPKP
IKTWVQAGVS ARLLNCLKKS GFEKPTPIQC QSLPVIMSGR DMIGIAKTGS GKTLAFLVPL
ARHLEHQAPL EPGDGPIALL LTPTRELALQ IYKEAKRLGQ TCGFRCVCVY GGTGISEQIA
DLKRGAEVIV CTPGRMIDML AANGGRVTNL RRTTYVVLDE ADRMFDLGFE PQVMRIVDNC
RPDRQTVMFS ATFPRQMEVL ARKALTLPIE VQVGGRSVVC SDVTQKVAVL QTEEEKVMKL
LELLGIYQEE GSVLVFVEKQ ESADELMRVL MNYGYPCLSL HGGIDQYDRD SVITDFKKGN
IRLLIATSVA ARGLDVADLV LVVNYDCPNH YEDYVHRCGR TGRAGKKGTA YTFITPDQEK
NSADLVKAFN ASGQMVPEDL YLMFQAYKER MMMEGKKVYS GSGSGFRGKG FRFDEVEAQL
ASDKRRFAKA ALGIEDSDDE GSGEGGSAGG VDWDSKIEDM FSSKRKVIDV AKSAAEANAS
TDSLDPKIAA QLELARQKAN QVALRGGLGT SASKTVLGGT AAAAAGGVPN AGRTAAELAA
ERLNAKLGYS KSSSIANADG DDEGGSAATN NATDFVRRYE EELEINDFPQ NVRWRITGRE
LLTHLNEYCD VGVSVRGVYI PQGKGISAAS AAAAAGLVDS SDERPLYLCL EATNERSIQL
AKAEIMRIIK EELVKLQSSS SLTNRGRYKV M
//
