ID   PRP5_NEOFI              Reviewed;        1193 AA.
AC   A1D373;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=NFIA_015590;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22866.1; -; Genomic_DNA.
DR   RefSeq; XP_001264763.1; XM_001264762.1.
DR   AlphaFoldDB; A1D373; -.
DR   SMR; A1D373; -.
DR   STRING; 36630.CADNFIAP00002011; -.
DR   PRIDE; A1D373; -.
DR   EnsemblFungi; EAW22866; EAW22866; NFIA_015590.
DR   GeneID; 4591228; -.
DR   KEGG; nfi:NFIA_015590; -.
DR   VEuPathDB; FungiDB:NFIA_015590; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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; Reference proteome.
FT   CHAIN           1..1193
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000282693"
FT   DOMAIN          588..766
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          793..943
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           557..585
FT                   /note="Q motif"
FT   MOTIF           714..717
FT                   /note="DEAD box"
FT   COMPBIAS        20..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..372
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         601..608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1193 AA;  131584 MW;  8D14028FB265D984 CRC64;
     MARHGDTRSP SPVGSTYSSS RRSRRDDDRY EKSRRDDGRS YRRSRSPERR YRDRDRDSYR
     RRDRSIDRRD DHRDEDSYRP SRRDRSRDRR RSRDRGDDRD HRRKSRERDY RSRRDDSRDR
     ARRRTDDSAD LKHKSRRDDS RTRNLDSKSR ETSKPSTPAP AAPTEDEKRA ERLAKLEAWK
     QKQAAERERK QREAAAAGGA RSILEEIDRK SGLSPAVGSP QSPAATPTTD ATPAPYAGKF
     DPKAIVRNAV PAPSTPAVLG NDVAVPQSAK ASASLSSMNN HVQANKPPAA ISTASSTLTV
     KRNVGGFGLG ARQVADAEKS SAVKTLGFGE EESKRKKLER LPTPPLEDAK DDTGAVDAAV
     EDEDDVDMQD GGTEEENAAA ARAAAERREE RLQSEALRAQ SKEAAPQPNG DVEMDDVSHQ
     AESEKMEVDA AEEEVDPLDA FMSELAETAP PKKTTGARFA KAKEQQPEAM FGDEHDVDLT
     AVGEGDADDF LAIANKAKKK KDIPAVDHEK MEYEPFRKKF YTEPSNLAEM TDEEAASLRL
     ELDGIKVRGV DVPKPVMKWS QCGLGVQTLD VIHRLGYENP TSIQSQAIPA IMSGRDVIGV
     AKTGSGKTIA FLIPMFRHIR DQRPLENMEG PIGLIMTPTR ELATQIHKDC KPFLKALNLR
     AVCAYGGAPI KDQIAELKRG AEIVVCTPGR MIDLLAANAG RVTNLRRVTY VVLDEADRMF
     DMGFEPQVMK IMANIRPDRQ TVLFSATFPR NMEALARKSL TKPIEIVVGG KSVVAPEITQ
     IVEVRNEDTK FVRLLEILGN LYSDDANEDA RALIFVDRQE AADTLLRELM RKGYPCMSIH
     GGKDQIDRDS TIEDFKAGIF PILIATSVAA RGLDVKQLKL VVNYDAPNHL EDYVHRAGRT
     GRAGNTGTAV TFLTEEQERY SVDIAKALRQ SGQKVPEPVQ KMVDSFLEKV KAGKEKASAS
     GFGGKGLERL DQERDAARMR ERRTYKTGEE GEDEEDKEDK AEKADERFSK VVSSVQSAAA
     AATTPLPGVP KGIDLDGKIT VHRTEKDPAG ASKNPLDKVG SAVADIHARL SRAGVMRSGV
     PIDNRGPDAG AFHATLEIND FPQKARWAVT NRTNVAKILE ATGTSITTKG SFYPAGKEPG
     PGENPKLYIL VEGETELAVT NAMRELMRLL KEGTLAAADS DARAPVGGRY NVV