ID   PRP5_CANGA              Reviewed;         816 AA.
AC   Q6FML5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; OrderedLocusNames=CAGL0K07029g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380957; CAG61490.1; -; Genomic_DNA.
DR   RefSeq; XP_448529.1; XM_448529.1.
DR   AlphaFoldDB; Q6FML5; -.
DR   SMR; Q6FML5; -.
DR   STRING; 5478.XP_448529.1; -.
DR   EnsemblFungi; CAG61490; CAG61490; CAGL0K07029g.
DR   GeneID; 2890388; -.
DR   KEGG; cgr:CAGL0K07029g; -.
DR   CGD; CAL0134379; CAGL0K07029g.
DR   VEuPathDB; FungiDB:CAGL0K07029g; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_2_1; -.
DR   InParanoid; Q6FML5; -.
DR   OMA; ANCLDVI; -.
DR   Proteomes; UP000002428; Chromosome K.
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:0000348; P:mRNA branch site recognition; IEA:EnsemblFungi.
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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..816
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000232360"
FT   DOMAIN          283..462
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          490..640
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           251..280
FT                   /note="Q motif"
FT   MOTIF           410..413
FT                   /note="DEAD box"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         296..303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   816 AA;  92283 MW;  13ECEE42B733164C CRC64;
     MTSIDKQKER LEKLARWKQK KSESKAVLNT QNVNTNSQSS NQNNVSDIEN KLEKVKAWKK
     RKLEVKSDQQ TPPATQSEIN HTSSVRLEEN IQGIKRKKRQ KRVSNVFDEV KPINSTPTND
     AQLSESDILE KVDLNTEDPL DSFFGNIETT EEFHFEVIDN KVNNDELLDE DNSKFDALQK
     EQKKLAKAKK NKNKKLLTPV NFRNIDLDPI SKCLYNEPEE IKSYTEDEIA DLRLDLDNIK
     IEGKDCPRPV TKWSQLGIPY DIIRFIKDVF SYKSLTPIQT QTIPAIMSGR DVIGISKTGS
     GKTISYLLPM IRHVKAQKKL RNGETGPIAV IFAPTRELAV QINEEVQKLI SDLDISSICC
     TGGSDLKKQI DKLKTGVEIA IATPGRFIDL LSLNGGNLVS TLRISFVVMD EADRLFDFGF
     EPQIASVLRT VRPDRQCVLF SATFPSKVSN FASRFLDSPL QITVNAEGMV NERINQKFTI
     CSDESDKFKE LLSLLKVFNS ETVDEKTIIF VSSQQICDII EKRLTDYSEK LYSIHAGRPY
     NERRQNLELF KKTSNSILLC TEVMSRGLNV PEVSRVILYN SAKTFAQYVH STGRTARGTR
     EGTSISLLLP NELSSAYILN KAMRDKDFSE CPVKEVKNLK QMAQKFEDGL KSGKYKLSTG
     LGGKGLENMD NSKETSNNDL DEQLKHQDNI SISQEADLPD DFKFDTSVET VTNADGTIAT
     VCKFVVNDLP QLVRWEMTKN TSISNMIRET GCSITLRGRY YPPSNVTNDN NTEPKLYLLI
     EATDDKAVRH CVDLLKDNAR VGFMKATSES LRNTKY