ID   PRP5_KLULA              Reviewed;         812 AA.
AC   Q6CKI1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; OrderedLocusNames=KLLA0F10505g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98266.1; -; Genomic_DNA.
DR   RefSeq; XP_455558.1; XM_455558.1.
DR   AlphaFoldDB; Q6CKI1; -.
DR   SMR; Q6CKI1; -.
DR   STRING; 28985.XP_455558.1; -.
DR   EnsemblFungi; CAG98266; CAG98266; KLLA0_F10505g.
DR   GeneID; 2895725; -.
DR   KEGG; kla:KLLA0_F10505g; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_2_1; -.
DR   InParanoid; Q6CKI1; -.
DR   OMA; ANCLDVI; -.
DR   Proteomes; UP000000598; Chromosome F.
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..812
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000232365"
FT   DOMAIN          277..456
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          481..639
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          45..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           245..274
FT                   /note="Q motif"
FT   MOTIF           404..407
FT                   /note="DEAD box"
FT   COMPBIAS        45..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         290..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   812 AA;  91154 MW;  0AF3B4F17D755C3E CRC64;
     MDQTEKLRIR QEKLAKWKKQ KLNNDVTASV SVDAKEERLK KLEAWKKKKK QQDELKQKDI
     KLTSIKSADR DRNKRRGQCS RKRPAFGGSD SESDDENSTS TLFKPRRNDT NTHVLTKDNS
     KDDLDDGNDA LDEYIHKLID KDSNTNRVRL IDNISEDEDA NDSSSEKTIS QEEAPVDSEI
     LFKKKGRKKI KAIDYSKVLN LITLNKCLYR EPNDLGLMSE KDVEELRLSL DNIKISGKDC
     PKPVTKWSQL GLSSEIMDLI SNELQFVTLT PIQCQAIPAI MSGRDVIGIS KTGSGKTVAF
     LLPLVRQIKA QPPLAPDETG PIGLILTPTR ELAVQIQEEA LKFCKGSGIS SICCVGGSEL
     KQQINELKRG VDIIVATPGR FIDLMTLNSG HLLSPTRISF VVMDEADRLF DLGFGPQVNQ
     IMGCIRPDKQ CVLFSATFPS KLKHFASRTL KNPIQITINS KSLINENIQQ RVQIFDEEHV
     KFEFLLKRLS DRLALHRGED EKTIIFVGSQ QLCDLLYDEL LLNGITTFPI HAGKPSAERL
     RNLQKFKETD NGILICTEVL SRGLNVPEVS LVIIYNAAKT IAQYVHTVGR TGRGTNNGVA
     LSFVMVDELA SAYILVKCMK ENELSSVPMV VYQKLKEMND EFSSGLKTGK YRLIQGFGGK
     GLDHLDELNE AKQSQEYTDY GVVENEEDVT EEESGATKME YTRGKREEGH STTYFAHINI
     NDLPQLARWE ATKTETVSNI KQETGCNFES KGSFYPEGKG PKNDTDDPKL YLIVEGAEES
     DVTMALELLN TKVKEGIRKA AVKDIQSGKY RM