ID   PRP5_ASPTN              Reviewed;        1181 AA.
AC   Q0D1K3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5;
DE            EC=3.6.4.13;
GN   Name=prp5; ORFNames=ATEG_00181;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476594; EAU38827.1; -; Genomic_DNA.
DR   RefSeq; XP_001210267.1; XM_001210267.1.
DR   AlphaFoldDB; Q0D1K3; -.
DR   SMR; Q0D1K3; -.
DR   STRING; 341663.Q0D1K3; -.
DR   PRIDE; Q0D1K3; -.
DR   EnsemblFungi; EAU38827; EAU38827; ATEG_00181.
DR   GeneID; 4354762; -.
DR   VEuPathDB; FungiDB:ATEG_00181; -.
DR   eggNOG; KOG0334; Eukaryota.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000007963; 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; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1181
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp5"
FT                   /id="PRO_0000282692"
FT   DOMAIN          580..758
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          785..935
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           549..577
FT                   /note="Q motif"
FT   MOTIF           706..709
FT                   /note="DEAD box"
FT   COMPBIAS        19..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..371
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..982
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         593..600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1181 AA;  130643 MW;  6F8FE77042F29318 CRC64;
     MARHGDTRSP SPVGSTHSSS RRSRRDDDRY ERTKRDDGRS YRRSRSPERR YRERDRESYR
     RRERSIARRD DYRDEDSYRP IRRDRSRDRR RSRDRGDDRD YRRRSRERDF RCRRDDSRDR
     ARRRADDSTD LKHKSRRDSS RDRPKDSASR SRETSKPATP APTAVPTDEE KRAERLAKLE
     AWKQKQAAER ERKQREAAAA GGARSLLDEI DRKSGLSPAV GSPQSPATPS TTADATPAPY
     AGKFDPKAIA KSAAPAQAAS NVLGDDVAVP TAVKASATST TTKVQANKPS TASKASAPLK
     AKGVVGRFGL GTKQAADMEK SSATKTLGFG EEESTRRKLE RLPTPPLDDA NDTNKPEDNA
     EDDDDVDMHE GDTEEQTAAA ARAAAERREE RLQNEASKTN GDTTMNDAPH SQEGEKMEVD
     AKEEEEIDPL DAFMSELVET APPKKTTGAK FSKAKEQQPE AIFGDENDPD ITAVGEGDAD
     DFLAIANKAK KKKDIPKVDH AKMEYEPFRK KFYTEPSDLA QMSEGELASL RLELDGIKVR
     GVDVPKPVQK WSQCGLGVQT LDVIDRLGYE NPTSIQSQAI PAIMSGRDVI GVAKTGSGKT
     VAFLIPMFRH IKDQRPLENM EGPIGLIMTP TRELATQIHK DCKPFLKALN LRAVCAYGGA
     PIKDQIAELK RGAEIVVCTP GRMIDLLAAN AGRVTNLRRV TYVVLDEADR MFDMGFEPQV
     MKIMANVRPD RQTVLFSATF PRNMEALARK TLNKPVEIVV GGKSVVAPEI TQIVEVRNED
     KKFVRLLELL GNLYSSDENE DARALIFVER QEAADTLLRE LMRKGYPCMS IHGGKDQIDR
     DSTIEDFKAG IFPVLIATSV AARGLDVKQL KLVVNYDAPN HLEDYVHRAG RTGRAGNTGT
     AVTFLTEDQE RFSVDIAKAL KQSGQKVPEP VQQMVDSFLE KVKAGKEKAS ASGFGGKGLE
     RLDQERDAAR MRERRTYKTG EEGEEEEEKE EKNEQAEERF NKVLSSVQSA SAPSLPGVPK
     GIDLDGKITV HRTEKDANGA KNPLDKVGSA VADIHARLSR AGVMRSGVPI DNRGPDAGAF
     HATLEINDFP QKARWAVTNR TNVAKILEAT GTSITTKGSF YPTGKEPGPG ENPKLYILVE
     GETELAVTNA MRELMRLLKE GTLAAADSDA RAPVGGRYNV V