ID A0A158PIH1_ANGCS Unreviewed; 827 AA.
AC A0A158PIH1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ACOC_LOCUS7554 {ECO:0000313|EMBL:VDM59139.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000755301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000755301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM59139.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM59139.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYYA01004051; VDM59139.1; -; Genomic_DNA.
DR STRING; 334426.A0A158PIH1; -.
DR WBParaSite; ACOC_0000755301-mRNA-1; ACOC_0000755301-mRNA-1; ACOC_0000755301.
DR OMA; FAQYVHT; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0043186; C:P granule; IEA:UniProt.
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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027}.
FT DOMAIN 179..207
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 210..388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 411..557
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 179..207
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 93103 MW; 72E7437B6FB73FFF CRC64;
ISTVHNWFQY SHPCETDKSE KKVWTLEDDD DDDPDDMVLD NSHNDLTDGG LKESTKDEED
PLDMFMSGLR KDLQKDRNSV IVTINAVKEK EKGVVLENEG RSDFVVDDID MEQAAASLCH
KGRMLPATDH SKVYYRPFRK DFYVETPEIA KMTKAEVRAY REELDGIEVK GNKCPKPIKT
WAQCGVEFKI LQQLKRHNYT KPTAIQAQAI PCIMAGRDII GIAKTGSGKT LAFLLPMFRH
ILDQPELEEL DGPIALIMSP TRELAMQTWK EANKFAKVLD IRVVCVYGGV GISEQIADLK
RGAEVIVCTP GRMIDMLAAN SGKVTNLRRV TYLVLDEADR MFDMGFEPQV MKIINNIRPD
RQTVLFSATF PRQMEALARK ILDKPIEIQS VVCADVTQNA IICEEHQKLL KLLELLGMYH
EQGNVIVFVD KQEKADDIVA QLMRNGYSCA PLHGGIDQFD RDSTITDFKS GVIKILVATS
VAARGLDVKN LILVVNYDCP NHYEDYVHRV GRTGRAGNKG YAYTFVLPEH QERMAGEVCR
AFETAGSKPP PELKAMFEKF KAEMAAQGKE VHLGGKGFAG SGYKYDEDEA EAEATKKKMT
RLVCGMEHGA DDDDELDEQL SMMIKSKRRV VEGQMSQSSL KKNADVEDKV AKAKAMAEKL
AMLRNLNAPA EKDAAQKTAE AIMKGGDIAP IEMTSKMIAK QLADKLNEKL NYLGGEALPT
TIQEEEWQYF EEELDINDFP QQVRYRVCSR ESLGHISEFA DVGISVKGSH YPPGKEPKEG
ERKLYLLLEA RHERNLKCAK EEIVRIMKDA FRQLVSEFNP VPRMVLL
//
