ID   PRP5_ASPFU              Reviewed;        1211 AA.
AC   Q4WT99;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=AFUA_1G10050;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000004; EAL90333.1; -; Genomic_DNA.
DR   RefSeq; XP_752371.1; XM_747278.1.
DR   AlphaFoldDB; Q4WT99; -.
DR   SMR; Q4WT99; -.
DR   STRING; 746128.CADAFUBP00000929; -.
DR   EnsemblFungi; EAL90333; EAL90333; AFUA_1G10050.
DR   GeneID; 3510546; -.
DR   KEGG; afm:AFUA_1G10050; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   InParanoid; Q4WT99; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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..1211
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000232357"
FT   DOMAIN          606..784
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          811..961
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          975..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           575..603
FT                   /note="Q motif"
FT   MOTIF           732..735
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..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1008
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         619..626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1211 AA;  133782 MW;  206E86EE324B2C8A CRC64;
     MARHGDTRSP SPVGSTYSSS RRSRRDDDRY EKSRRDDLRS YRRSRSPERR YRDRDRDSYR
     RRDRSVDRRD DHRDEDSYRS SRRDRSRDRR RSRDRGDDRD HRRKSRERDY RSRRDDSRDR
     ARRRTDDSAD LKHKSRRDDS RTRNLDSKPR EASKPSTPAP TAPTEDEKRA ERLAKLEAWK
     QKQAAERERK QREAAAAGGA RSILEEIDRK SGLSPAVGSP QSPATPTTDA TPTPYSGKFD
     PKAIVRNAAP APSTPAVLGN DVAVPQSAKA SASSSSMNNH VQANKHPAAN STTSCKLYIP
     TIRFLQIANV TCTATSTVKR NVGGFGLGAK QVADAEKSSA VKTLGFGEEE SKRKKLERLP
     TPPLEDAKDD MGAVDAAVED EDDVDMQDGG TEEENAAAAR AAAERREERL QSEALRAQSK
     EAALQSNGDV EMNDVPHQAE SEKMEVDAAE EEVDPLDAFM SELAETAPPK KTTGARFTKA
     KDQQPEAMFG DEHDVDLTAV GEGDADDFLA IANKAKKKKD IPTVDHEKME YEPFRKKFYT
     EPSNLAEMTD EEAASLRLEL DGIKVRGVDV PKPVMKWSQC GLGVQTLDVI QKLGYENPTS
     IQSQAIPAIM SGRDVIGVAK TGSGKTIAFL IPMFRHIRDQ RPLENMEGPI GLIMTPTREL
     ATQIHKDCKP FLKALNLRAV CAYGGAPIKD QIAELKRGAE IVVCTPGRMI DLLAANAGRV
     TNLRRVTYVV LDEADRMFDM GFEPQVMKIM ANIRPDRQTV LFSATFPRNM EALARKSLTK
     PIEIVVGGKS VVAPEITQIV EVRNEDTKFV RLLEILGNLY SDDANEDARA LIFVDRQEAA
     DTLLRELMRK GYPCMSIHGG KDQIDRDSTI EDFKAGIFPV LIATSVAARG LDVKQLKLVV
     NYDAPNHLED YVHRAGRTGR AGNTGTAVTF LTEEQERYSV DIAKALRQSG QKVPEPVQKM
     VDSFLEKVKA GKEKASASGF GGKGLERLDQ ERDAARMRER RTYKTGEEGE DEEDKEDKAE
     KADERFSKIV SSVQSAAAAA TTPLPGVPKG IDLDGKITVH RTEKDPAGAS KNPLDKVGSA
     VADIHARLSR AGVMRSGVPI DNRGPDAGAF HATLEINDFP QKARWAVTNR TNVAKILEAT
     GTSITTKGSF YPAGKEPGPG ENPKLYILVE GETELAVTNA MRELMRLLKE GTLAAADSDA
     RAPVGGRYNV V