ID   PRP5_ASPCL              Reviewed;        1192 AA.
AC   A1CQA9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=ACLA_025470;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW07830.1; -; Genomic_DNA.
DR   RefSeq; XP_001269256.1; XM_001269255.1.
DR   AlphaFoldDB; A1CQA9; -.
DR   SMR; A1CQA9; -.
DR   STRING; 5057.CADACLAP00002222; -.
DR   PRIDE; A1CQA9; -.
DR   EnsemblFungi; EAW07830; EAW07830; ACLA_025470.
DR   GeneID; 4701879; -.
DR   KEGG; act:ACLA_025470; -.
DR   VEuPathDB; FungiDB:ACLA_025470; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000006701; 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..1192
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000282690"
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..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..1003
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..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..374
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..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   1192 AA;  131673 MW;  2CDE07E011185610 CRC64;
     MARHGDTRSP SPVGSTYSSS RRSRRDDDRY EKSRREDGRG HRRSRSPERR YRDRDRDRES
     YRRRDRSLDR RDDYRNDGGY RSNRRDRSRD RRRSRDRGDD RDHRRRSRDR DYRSRRDDSR
     DKARRRTDDS ADLKHKSRRD DSRTRDLDSK SRDTSKPSTP APAAQTEDEK RAERLAKLEA
     WKQKQAAEKE RKQREAAAAG GARSILEEID RKSGLSPAVG SPKSPVTPTT DATPAPYAGK
     FDPKAIKRNA APTPSAPLVL GNDVAVPQIA KASATFSSMN NHAQANKPAA ALSTAPSTLK
     SKRNVGGFGL GAKQVADAEK PSAVKTLGFG EEESTRKKLE RLPTPPLEDG KDETVAADMG
     AEDEDDDMQD GETEEENAAA ARAAAERREE RLQNEALRAQ SSEKVPQTNG DVEMNDAPIQ
     AEAENMEVDV EEEDVDPLDA FMSELAESAP PKKTFGTKFS KAKEQQPEAM FGDENDVDLT
     AVGEGDADDF LAIANKAKKK KDIPTVNHEK VEYEPFRKKF YTEPSNLAQM TDEEAASLRL
     ELDGIKVRGV DVPKPVQKWS QCGLGVQALD VIERLGYESP TSIQSQAIPA IMSGRDVIGV
     AKTGSGKTVA FLIPMFRHIK DQRPLDNMEG PIGLIMTPTR ELATQIHKDC KPFLKALNLR
     AVCAYGGAPI KDQIADLKRG AEIVVCTPGR MIDLLAANAG RVTNLRRVTY VVLDEADRMF
     DMGFEPQVMK IMANIRPDRQ TVLFSATFPR NMEALARKAL TKPIEIIVGG RSVVAPEITQ
     IVEVRNEDTK FVRLLEILGN LYSDDANEDA RSLIFVERQE AADALLRELM RKGYPCMSIH
     GGKDQIDRDS TIEDFKAGIF PVLIATSVAA RGLDVKQLKL VVNYDAPNHL EDYVHRAGRT
     GRAGNTGTAV TFLTEEQERY SVDIAKALKQ SGQQVPEPVQ KMVDSFLEKV KAGKEKASAS
     GFGGKGLERL DQERDAARNR ERRTYKTGEE GEDEEEKEDK AEKADERFNK ALSSVQSAAA
     AAPTLPGVPK GIDLDGKITV HRTEKDPAGT SKNPLDKVGS AVADIHARLS RAGVMRSGVP
     IDNRGPDAGA YHATLEINDF PQKARWAVTN RTNVAKILEA TGTSITTKGS FYPPGKVPGP
     NENAKLYILV EGETELAVTN AMRELMRLLK EGTIAAADSD ARAPVGGRYN VV