ID   PRP28_PICST             Reviewed;         482 AA.
AC   A3LNL1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE            EC=3.6.4.13;
GN   Name=PRP28; ORFNames=PICST_75833;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000496; ABN64351.2; -; Genomic_DNA.
DR   RefSeq; XP_001382380.2; XM_001382343.1.
DR   AlphaFoldDB; A3LNL1; -.
DR   SMR; A3LNL1; -.
DR   STRING; 4924.XP_001382380.2; -.
DR   PRIDE; A3LNL1; -.
DR   EnsemblFungi; ABN64351; ABN64351; PICST_75833.
DR   GeneID; 4836914; -.
DR   KEGG; pic:PICST_75833; -.
DR   eggNOG; KOG0333; Eukaryota.
DR   HOGENOM; CLU_003041_11_4_1; -.
DR   InParanoid; A3LNL1; -.
DR   OMA; KKFNFEW; -.
DR   OrthoDB; 820037at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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..482
FT                   /note="Pre-mRNA-splicing ATP-dependent RNA helicase PRP28"
FT                   /id="PRO_0000285144"
FT   DOMAIN          88..288
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          321..473
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           56..85
FT                   /note="Q motif"
FT   MOTIF           220..223
FT                   /note="DEAD box"
FT   BINDING         101..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   482 AA;  54612 MW;  A0772EA4BD220375 CRC64;
     MMALEPVSTT RDNIDFVETT HWSEKSLDQM TARDWRIFRE DYGITSKGGD IDNPLRTWNE
     ASIPSKLLSI IVDKLEYLEP TPIQRAAIPL ALNQRDVVGI AETGSGKTLA FLIPLLSYIL
     NTDKNYLEYE HQQEQNYNKP LGLILAPTRE LAQQITKEAQ KFGDRLGLNV VSIIGGHQYE
     ETVHSIRTGV HVVVATPGRL VDSLERNIIG LDKCYYLIMD EADRMIDMGF EKALQSILSY
     VPSTDRLNST IDSMIFHIKK RITLMFTATI SPPIEKITKN FLIKPGYLYI GGAGEALDHI
     VQNFEYLGSA TGGSEDFDSK RFDKLVRIIQ QHSRESRQFS IIIFANYKRV CDLLSLELEK
     NGFRDNVVIH GSKTQELREK AISSFRSHES RILIATDVAA RGIDVPNVSL VVNFQMSRKF
     DEYVHRIGRT GRAGNRGESY TFIDDSDSDV FIDLKKFLVN GGKKCPDWLI KHASTQSQVL
     RD