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Database: UniProt
Entry: A5E058
LinkDB: A5E058
Original site: A5E058 
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   16-OCT-2019, entry version 67.
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 /
OS   NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL 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.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
RA   Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
RA   Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
RA   Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
RA   Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
RA   Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
RA   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
CC       and in nuclear splicing. Catalyzes an ATP-dependent conformational
CC       change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2
CC       snRNP 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH981526; EDK44816.1; -; Genomic_DNA.
DR   RefSeq; XP_001526437.1; XM_001526387.1.
DR   SMR; A5E058; -.
DR   STRING; 36914.XP_001526437.1; -.
DR   PRIDE; A5E058; -.
DR   EnsemblFungi; EDK44816; EDK44816; LELG_02995.
DR   GeneID; 5233354; -.
DR   KEGG; lel:LELG_02995; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   eggNOG; ENOG410XSQV; LUCA.
DR   InParanoid; A5E058; -.
DR   KO; K12811; -.
DR   OMA; RGIDCPK; -.
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: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   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; Complete proteome; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN         1    994       Pre-mRNA-processing ATP-dependent RNA
FT                                helicase PRP5.
FT                                /FTId=PRO_0000294648.
FT   DOMAIN      419    597       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      629    780       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     432    439       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED       20     87       {ECO:0000255}.
FT   COILED      217    284       {ECO:0000255}.
FT   COILED      310    382       {ECO:0000255}.
FT   MOTIF       387    416       Q motif.
FT   MOTIF       545    548       DEAD box.
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
//
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