ID   PRP5_CRYNB              Reviewed;        1072 AA.
AC   P0CQ99; Q55XI8; Q5KME7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE            EC=3.6.4.13;
GN   Name=PRP5; OrderedLocusNames=CNBB3750;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000010; EAL22497.1; -; Genomic_DNA.
DR   RefSeq; XP_777144.1; XM_772051.1.
DR   AlphaFoldDB; P0CQ99; -.
DR   SMR; P0CQ99; -.
DR   PRIDE; P0CQ99; -.
DR   EnsemblFungi; AAW41818; AAW41818; CNB01970.
DR   EnsemblFungi; EAL22497; EAL22497; CNBB3750.
DR   GeneID; 4934469; -.
DR   KEGG; cnb:CNBB3750; -.
DR   VEuPathDB; FungiDB:CNBB3750; -.
DR   HOGENOM; CLU_003041_0_2_1; -.
DR   Proteomes; UP000001435; Chromosome 2.
DR   GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990446; F:U1 snRNP binding; IEA:EnsemblFungi.
DR   GO; GO:1990447; F:U2 snRNP binding; IEA:EnsemblFungi.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; 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; 1.
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.
FT   CHAIN           1..1072
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000410260"
FT   DOMAIN          434..612
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          639..790
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           403..431
FT                   /note="Q motif"
FT   MOTIF           560..563
FT                   /note="DEAD box"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         447..454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1072 AA;  119710 MW;  D761996C4D4C3E43 CRC64;
     MPRSPYRSSN RSYRSPSPSR YDRSHPSSSS RRQDDRKASR YDDDYSRDRE RDRERERDRT
     RDYRDRDRDY DRRRDKDRYR DDDRDRRRRD DKDDRRREER DRGSDRKRDS ERRSPMSTIR
     VDPIVSLASP VPETEEEKKR KAKERLETWK RQRALKEGKS AAATPEPKST APPPVTSGLP
     PKPTAFSLSR IGLPLKPTNP TPLKRSMAAL DDEDTSDRKL QKLDLPDFDP EVQSGDAAQV
     GSIGADLAVA DGDEDDDTVV KKEEEKEEKM DIDKKAEEDE EEDPLDAFMR DNVQQVVEVN
     KADAKRMGLR VAEDGSDDEN QGQVVEKDKL AEAEALLQQA AAKSRKKDLP PPDHSKIDYE
     PFRKAFYVPP VEVLEMDEEE AELVRLEMDG IKIRGQDAPK PVRNWGAFGL PQGCLDVIKH
     QGWETPTSIQ AQAIPAIMSG RDVIGIAKTG SGKTVAFLLP MLRHVRDQRP VSGSEGPIAV
     VMSPTRELAS QIYKECQPFL KVLNIRASCC VGGSSISEDI AAMKKGAEVV ICTPGRMIDL
     LTANNGRVTN VRRTTYIVMD EADRMFDMGF EPQVMKIINN VRPSAQKVLF SATFPKTMES
     LARRILVKPL EITVGGRSVV APEIDQRVEV RDGDTKFTRL LEILGEMGEE HKDEDDFRTL
     IFVDRQESAD DLFRELLQRG YVCASLHGGK EQVDRDEAIK NFKNGDVPII VATSVAARGL
     DVKELKLVIN YDAPNHMEDY VHRAGRTGRA GNKGTCITFI TPEQERFSVD IVRALEASKA
     FIPDDLKKMS DSFLGKIKSG KARAAGSGYS GKGLERIERR REEKDRAEKT TYGDTSEALS
     LSSREGAVIP YKAKTNEFKP PETSHKGEAD YTFTEIKVDI VNGPAPDRVS SQPVFNPKNA
     VASLPAQTLA ALEKAKKEGR GVDAANLANV VAKLTQSIEL TKAEKLGLAA ATSAPRLAPG
     ARTKDPDATD WHAIFPINDY PQKARWKATN KEQMTLLQEV SGASITMRGR FYPPGEEPAL
     GGEPKLSLLI ESNDEMRVRA AVEEIRRVLV EGSVQALNAV DRAGASGGRY AV