ID   PRP5_COCIM              Reviewed;        1197 AA.
AC   Q1DHB2; J0HHG7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, 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=CIMG_10301;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704915; EAS27696.3; -; Genomic_DNA.
DR   RefSeq; XP_001239279.1; XM_001239278.2.
DR   AlphaFoldDB; Q1DHB2; -.
DR   SMR; Q1DHB2; -.
DR   STRING; 246410.Q1DHB2; -.
DR   PRIDE; Q1DHB2; -.
DR   EnsemblFungi; EAS27696; EAS27696; CIMG_10301.
DR   GeneID; 4557762; -.
DR   KEGG; cim:CIMG_10301; -.
DR   VEuPathDB; FungiDB:CIMG_10301; -.
DR   InParanoid; Q1DHB2; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; 2.
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..1197
FT                   /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT                   /id="PRO_0000256034"
FT   DOMAIN          590..768
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          795..945
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          956..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           559..587
FT                   /note="Q motif"
FT   MOTIF           716..719
FT                   /note="DEAD box"
FT   COMPBIAS        18..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..381
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..1011
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         603..610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1197 AA;  133147 MW;  8C3DD6347E2886FB CRC64;
     MARETRSPSP VGSTHSSSKR SRRNDDYLDR SRRDDGRGHR RSRSPPRRHR DRDWDRHRDR
     DRDRDRDRVR DRERGRDRER DRDTYRKSDR SVDRRDYRDD VRDDTSYRPS RRDRSRPRYH
     SRDREDGREY RHRSRDRRRR DDSADSKSIA KRNESRDRVS SKDFTGKSRE VSKPSTPAPP
     IAQTDEEKKA ERLAKLEAWK QKQAAEKERK QKELAAAGGA RSILAEIDKR STLRQAGVSQ
     ETPAPQESES ASAKKFDPKT ITKNAAAQPE RLSLLGNDVA VPNTTTSSEV AGRNGADSTR
     IAPLKPRGNV SGFGFGAKSA AELEKASHKR ALDFGDEESS RKKLMKLPDP SLEDNDTPNG
     TVNGAEEEED DDGDIDMQDG GTEEENAAAA RAAAEKREER LQNQTVALES QPEQQPETLE
     TDQNGSAEPM DVEDEEEIDP LDAFMSGLKD SVTVDASKYR KNVSKPKQEP EAIFGDEDDV
     DLKAMDFEAD DFLAITSKTR KKKDLPTVNH ETIDYEPFRK SFYTEPVDLA ELNDEEVAAL
     RLELDGIKVR GVDVPKPVQK WSQCGLGVQT LDVIRKLGYE QPTSIQSQAI PAIMSGRDVI
     GVAKTGSGKT IAFLLPMFRH IKDQRPLENM EGPVGLIMTP TRELATQIHK ECKPFLKALN
     LRAVCAYGGA PIKDQIAELK RGAEIIVCTP GRMIDLLAAN SGRVTNLRRV TYVVLDEADR
     MFDMGFEPQV MKIISNIRPS RQTVLFSATF PRNMEALARK TLTKPVEIIV GGRSVVAQEI
     TQIVEVRPEN TKFVRLLELL GNLYSDDNNE DARALIFVDR QEAADGLLRD LMRKGYPCMS
     IHGGKDQVDR DSTIDDFKAG IFPVLIATSV AARGLDVKQL KLVINYDAPN HLEDYVHRAG
     RTGRAGNTGT AVTFLTEEQE RYSVDIAKAL KQSGQSVPEA VQKMVDSFLE KVKSGKEKAS
     ASGFGGKGLE RLDQERDAAR NRERKTYKTG EEGEEDEEKE KKEKDKGEEL FAKAASAVQS
     SSAPTPSATP GVPKGIDLDG KITVHKTERA TPSTTGTNPL DKVGSAVADI HARLNKAGVM
     RSGVPIDNKG PDAGAFHATL EINDFPQKAR WAVTNRTNVA KILEATGTSI TTKGSYYPPG
     KEPGPNENPK LYILVEGDTE LVVTNAMREL MRLLKEGTIA AADSEARAPA SGRYNVL