ID   PRP28_CANAL             Reviewed;         581 AA.
AC   Q59W52; A0A1D8PF71;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE            EC=3.6.4.13;
GN   Name=PRP28; OrderedLocusNames=CAALFM_C111300CA;
GN   ORFNames=CaO19.672, CaO19.8289;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May
CC       destabilize the U1/5'-splice site duplex to permit an effective
CC       competition for the 5'-splice site by the U6 snRNA, resulting in the
CC       switch between U1 and U6 at the 5'-splice site. May also act to unwind
CC       the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC       the first covalent step of splicing (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   -!- SUBUNIT: Component of the U5 snRNP complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP017623; AOW26755.1; -; Genomic_DNA.
DR   RefSeq; XP_713805.2; XM_708712.2.
DR   AlphaFoldDB; Q59W52; -.
DR   SMR; Q59W52; -.
DR   BioGRID; 1227585; 1.
DR   STRING; 237561.Q59W52; -.
DR   PRIDE; Q59W52; -.
DR   GeneID; 3644552; -.
DR   KEGG; cal:CAALFM_C111300CA; -.
DR   CGD; CAL0000181927; orf19.8289.
DR   VEuPathDB; FungiDB:C1_11300C_A; -.
DR   eggNOG; KOG0333; Eukaryota.
DR   HOGENOM; CLU_003041_11_4_1; -.
DR   InParanoid; Q59W52; -.
DR   OrthoDB; 820037at2759; -.
DR   PRO; PR:Q59W52; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; 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:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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   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; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..581
FT                   /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT                   /id="PRO_0000232371"
FT   DOMAIN          199..396
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          424..575
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           168..196
FT                   /note="Q motif"
FT   MOTIF           328..331
FT                   /note="DEAD box"
FT   COMPBIAS        44..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         212..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   581 AA;  65641 MW;  DAE95408BF543F81 CRC64;
     MSSNIFKRFK SAEESLDEDE SVTPVYIPKA KRAKLEALKA KKSQIASRLS THKQQSAPTT
     TTNTSTTAST TTTATTNNTN NSKPSIQTKK PTGKKFQFDW DVEEEDTASG FVPLIEMDEE
     IDDPLFSGQE STHWTNKNLE EMTDRDWRIF KEDYNITTKG KNIPNPLRYW NEGSINDKLV
     SIISQLGYEE PTSVQRASIP LALKKRDVVG VAETGSGKTL AFLIPVLNYI LSIDENYLKY
     EKISNEPVGL ILAPTRELAL QITKEAEKFC KKLGYQVLPI IGGHHYQDTI NKIDQTGVHL
     IVATPGRLVD SIERKIVDLS KCYCLVMDEA DRMIDMGFEK DLNKVLDKLP TEKQLSSTID
     GRIFHLEKRS TMMFTATISP TVEKLTKKYL IDPGYLYIGG AGEALDNISQ SFEFLSSATT
     EATKFNKLIK IIRSHWRVTE NPLIIIFANF KHVCDSLSQE LSSNDINNVV IHGSKSQDMR
     EQAITNFRNH ESEVLIATDV AARGIDIPNV TLVINYQMVK KFDEYIHRIG RTGRAGNLGE
     SFTFISDQDT EIFTPLKKFL KKGGKRLPDW LYKHQSQTVQ E