ID   PRP5_LODEL              Reviewed;         994 AA.
AC   A5E058;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; ORFNames=LELG_02995;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH981526; EDK44816.1; -; Genomic_DNA.
DR   RefSeq; XP_001526437.1; XM_001526387.1.
DR   AlphaFoldDB; A5E058; -.
DR   SMR; A5E058; -.
DR   STRING; 379508.A5E058; -.
DR   EnsemblFungi; EDK44816; EDK44816; LELG_02995.
DR   GeneID; 5233354; -.
DR   KEGG; lel:LELG_02995; -.
DR   VEuPathDB; FungiDB:LELG_02995; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_2_1; -.
DR   InParanoid; A5E058; -.
DR   OMA; ANCLDVI; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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   Gene3D; 3.40.50.300; -; 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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Coiled coil; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..994
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000294648"
FT   DOMAIN          419..597
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          629..780
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..87
FT                   /evidence="ECO:0000255"
FT   COILED          217..284
FT                   /evidence="ECO:0000255"
FT   COILED          310..382
FT                   /evidence="ECO:0000255"
FT   MOTIF           387..416
FT                   /note="Q motif"
FT   MOTIF           545..548
FT                   /note="DEAD box"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         432..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   994 AA;  112203 MW;  E2561560AC0A65B5 CRC64;
     MTLPSGDSSI TNNTNQTLNE DEKRRLRREK LAALRQKKLA EAQNGEGNKR QEGNGNGTGQ
     GTGNVAADLT TKRNEKQKVE NSFAKLNSTS IDHSSTETQA TSLEEKQRLL LKRQGQRIED
     WKKNRSADTA SHFPQRAKEN LSHTRIAITK KSTFKLPKIK RNNNKRVFGF VNEDKEGGGG
     KEEEDEEEEF TKKKILKIAN DDARDYLNYG EKFRKPVLEE AEDDLDQFIE SISKSESFVD
     NNNGGKQVQE QNVEEEKQQQ QQQQLEQEQE QEQEQLEKLP RYLAVNNNNN EDTDEVYRYE
     EDFDDEFDED DEDDINKRLS AKLNKLQNTA KELKEIDHTS IEYPKFRKHF YQVPFEMSTM
     DNRELDMLRL ELDNVRARGK NVPPPFLTWG QLLMPESVMS VIQNDLGFAK PSPIQCQAIP
     IVLSGRDMIG VAKTGSGKTL SYVLPMVRHI QDQLFPKPGE GPIGLVLSPT RELALQIEKE
     ILKFSSTMDL KVCCCYGGSN IENQISELKR GVNVIVATPG RLIDLLAANG GRITTLRRTT
     FVVLDEADRM FDMGFEPQIQ KIFTQIRPDK QTVLFSATFP RKLEQLAKKV LHNPIEIIVG
     GVSVVASEIS QEIILFEDTD QLMNHKIQKL EDILSRFFDL GKNTGKVLVF VEKQTDADKL
     VSVLLKKAIP CIAIHGGKDQ IDRKHAIREF SDDQSGINVL IATSIAARGL DVRNLDLVVN
     FEPPSHLEDY VHRVGRTGRA GKHGEAITFV DNTQEKEISI LVKALKMSSR AVDSKLQEIA
     DKFMKKIESG EEKRSSGFGG KGLEKLQNVR ETNMQLQKKM FGNFKKEDGK KSHRDLSEQV
     DYFGSSSSSS SFPSSSNTTT TTTTTSTASA IEIPTFEIIE GNSPETSGPD KCKFYCRVTI
     NDLPQKVRWG IVQRESLSKI IEASKTSITT RGQFYPPQSK QTPTNDQPKL YLLIEGLTRK
     AVEEAAVLIR DKMLQGVEAM RLDNHSAPTG RYVV