ID   PRP16_SCHPO             Reviewed;        1173 AA.
AC   Q9P774; Q9UUE8;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16;
DE            EC=3.6.4.13;
GN   Name=prp16; ORFNames=SPBC1711.17, SPBC17G9.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase involved in pre-mRNA
CC       splicing. {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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       PRP16 sub-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; CU329671; CAB88247.1; -; Genomic_DNA.
DR   PIR; T39724; T39724.
DR   RefSeq; NP_595890.2; NM_001021796.3.
DR   AlphaFoldDB; Q9P774; -.
DR   SMR; Q9P774; -.
DR   BioGRID; 276550; 13.
DR   IntAct; Q9P774; 3.
DR   STRING; 4896.SPBC1711.17.1; -.
DR   MaxQB; Q9P774; -.
DR   PaxDb; Q9P774; -.
DR   PRIDE; Q9P774; -.
DR   EnsemblFungi; SPBC1711.17.1; SPBC1711.17.1:pep; SPBC1711.17.
DR   GeneID; 2540006; -.
DR   KEGG; spo:SPBC1711.17; -.
DR   PomBase; SPBC1711.17; prp16.
DR   VEuPathDB; FungiDB:SPBC1711.17; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   eggNOG; KOG0924; Eukaryota.
DR   HOGENOM; CLU_001832_6_1_1; -.
DR   InParanoid; Q9P774; -.
DR   OMA; VMFHRSP; -.
DR   PhylomeDB; Q9P774; -.
DR   Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-SPO-72187; mRNA 3'-end processing.
DR   PRO; PR:Q9P774; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR   GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; ISO:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1173
FT                   /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT                   prp16"
FT                   /id="PRO_0000055149"
FT   DOMAIN          502..665
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          687..862
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          152..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           612..615
FT                   /note="DEAH box"
FT   COMPBIAS        152..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         515..522
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1173 AA;  132971 MW;  1B382AC72F2C2249 CRC64;
     MLSHNQNDLL FTKLIDKLTD YMSSKDAATS LASRVLTIAK GSSSSTEFSN ALHTFGRFSD
     NDSVLIYDLC KSIIGLETNL GISKDKLPGN DGSQVAGLVL SNRSGLKGRE PKKSQLGLDV
     LAVQKKKEKS QVEGRSELSQ VENDSLESIG NYDRVEFKRP KNPHEKHFRP LRQRSSVDDH
     QEFESEDDKY RRNSYSSWSG SNFESSNGSN RRRYRTQMEE PLSSKRRNRF GNGSRRDVDS
     SKYSHDSDYS YGAHSSWDAR DVEYPEEDPE SKADRQRWEE EQAHLDRDWY MNSESQNLLG
     DEVHNPFSDF ETVEDRAHEA EFIEKQKKHL SIEASDRFKE NSMWEKNRMI TSGVSKAPGL
     ESDYSLMEER RVHLLVDELR PHFLDGAEFS SKKVGDITSV RDPQSDLAIN ARLGSRLVRE
     RREFRERQKA ASAATSLAGT SLGNVMGLKD SNDEDAKAGT TPVKVAGRSE QSNKKDTEFA
     RTKSYREQRE FLPAFAVREQ LLSVIRDNQV LIVVGETGSG KTTQLAQFLY EDGYHRNGMI
     GCTQPRRVAA MSVAKRVSEE MGVRLGSTVG YSIRFEDVTG PDTVIKYMTD GVLLRESLMQ
     NNLEKYSVII MDEAHERSLN TDILMGLLKK VLSRRRDIKL LVTSATMNSQ KFSDFFGGAP
     QFTIPGRTYP VDIMFAKAPC SDYVEAAVRQ VLQIHLSQPA GDILVFMTGQ EDIEATCEII
     ADRLNQLHDA PRLSILPIYS QMPADLQAKI FDSAEPGVRK VVVATNIAET SLTVHGISYV
     VDTGYCKLKM YNSKLGIDTL QVTPISQANA NQRAGRAGRT GPGIAYRLYT EMAYIREMFE
     TTLPEIQRTN LSNTVLILKS LGVEEISDFD FMDRPPNDTL MASLYELWTL GALDNFGKLT
     TLGKKMSLFP MDPSLSKLII IAEDYKCTEE IITIVSMLSV PSVFYRPKER AEESDAAREK
     FNVPESDHLM LLNIYQHWQR NGYSNSWCSK HFLHSKTLKR ARDIRQQLVE IMSKQKISLE
     SVSDWDIVRR VLCSAYFHQA ACAKGIGEYV HLRSGMPCHL HVTSSLYGLG YLPDYVIYHE
     LVLTSKEYMN IVTSVDPYWL AEFGGVYYSV KERFRNETES YDRVFSSKPQ LDAQIAADRE
     LDAKQKLAKN QEPVKSKRKS VIRAKPPRRV RGF