ID   PRP5_NEUCR              Reviewed;        1194 AA.
AC   Q7SH33;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp-5;
DE            EC=3.6.4.13;
GN   Name=prp-5; ORFNames=B12J7.200, NCU02696;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX842635; CAE76515.1; -; Genomic_DNA.
DR   EMBL; CM002236; EAA36233.1; -; Genomic_DNA.
DR   RefSeq; XP_965469.1; XM_960376.2.
DR   AlphaFoldDB; Q7SH33; -.
DR   SMR; Q7SH33; -.
DR   STRING; 5141.EFNCRP00000002040; -.
DR   PRIDE; Q7SH33; -.
DR   EnsemblFungi; EAA36233; EAA36233; NCU02696.
DR   GeneID; 3881603; -.
DR   KEGG; ncr:NCU02696; -.
DR   VEuPathDB; FungiDB:NCU02696; -.
DR   HOGENOM; CLU_003041_0_3_1; -.
DR   InParanoid; Q7SH33; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..1194
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase prp-
FT                   5"
FT                   /id="PRO_0000232366"
FT   DOMAIN          592..770
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          797..945
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           561..589
FT                   /note="Q motif"
FT   MOTIF           718..721
FT                   /note="DEAD box"
FT   COMPBIAS        17..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1026..1040
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         605..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1194 AA;  131302 MW;  34C92267AAE8CC71 CRC64;
     MARLRDSRSP SPAGSLSARK RKDDDRRDRD RRDGPVDHRR RSRSPIDRRY RDRDRDRGRD
     GRDRDSYRRR DRSIDRRDDD YYRGSRRDGD RRRSRDRGLD RLRSPDRRRD RSRDPDREYR
     PRRDDSRDRA RVRREGTAES SSHRRDDVRA RDQPKPGNTT AKENEPAKST PTQPQTEAEK
     KAERLRKLQA MKQKHALKEA KEADVTAGLT RKLFMEMDQR ASGAVVGSGT NSPAPASPAA
     AESPASPAPY VGKFDPKAIA RNAKPARASS PVRLGDVKLG DVKVGAPVAA AASIAGQGKG
     AASGKAGLLQ TGRPISTFGF NKSADALKTT AKRKIDMGDE EIIKRKLVKL PDLALENADD
     TPYADDDVAE DAEKDFDVLL AGTEEDRAEA QRLLRERREE QIQKESMAME IDSAPSNIEV
     ATEPVAQNPT AMDVDDEVDP LDAFMAGLEQ TASGEESHSK ADTLTEKKNG NIPPEAYFSD
     DDYGYEADGT DPTSILAMAS KKKKKDIPTI DYSKLDLNPI RKNFWVEPYE LSHMSEEELA
     ELRLELDGIK VSGKNIPKPV QKWSQCGLTR PILDTIESLG FEKPTPIQMQ ALPVIMSGRD
     VIGVAKTGSG KTMAFALPML RHVKDQDPVT GDDGAIALIM TPTRELCTQI YSDLQPFAKA
     LKLRVVAAYG GNAIKDQIAE LKRGAEIIVA TPGRLIDLLA ANGGRVTNLK RATYLVLDEA
     DRMFDMGFEP QVMKIFNNVR PDRQTILFSA TMPRIIDALT KKVLRDPVEI TVGGRSVVAP
     EITQIVEVMD EGKKFNRLLE LLGELYADDD DVRSLIFVER QEKADDLLRE LLRRGYGCMS
     IHGGKDQEDR NSTISDFKKG VCPILIATSI AARGLDVKQL KLVINYDAPN HLEDYVHRAG
     RTGRAGNTGT AVTFITEEQE NCASGIAKAL EQSGQPVPDR LNEMRKAWKE KVKAGKAKDA
     SGFGGKGLEK LDKDREAARM RERKTHKAEG EEDDVKEDAP AEDGEKKDKT KVAIQSAVSA
     IVSRDASKAE TEDKHAIPAG AVKAGHHASS GKSGGALDKA ASAISEINAR LARAGQLRPG
     QPIDNKGPDA GAFHATLEIN DFPQKARWAV TNRTNVAKIL EATGTSITTK GNYYAPGKEP
     GPGQEPKLYI LIEGDTEVVV GNALSELTRL LREGTMAAAD AESRAPASGR YTIT