PRP22_SCHPO
ID PRP22_SCHPO Reviewed; 1168 AA.
AC O42643;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase prp22;
DE EC=3.6.4.13;
GN Name=prp22; ORFNames=SPAC10F6.02c;
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).
RN [2]
RP FUNCTION.
RX PubMed=15452114; DOI=10.1074/jbc.m408815200;
RA Sapra A.K., Arava Y., Khandelia P., Vijayraghavan U.;
RT "Genome-wide analysis of pre-mRNA splicing: intron features govern the
RT requirement for the second-step factor, Prp17 in Saccharomyces cerevisiae
RT and Schizosaccharomyces pombe.";
RL J. Biol. Chem. 279:52437-52446(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
CC -!- FUNCTION: Acts late in the splicing of pre-mRNA. Required for the
CC splicing of introns with a branch nucleotide to 3'-splice site distance
CC greater or equal to 15. Mediates the release of the spliced mRNA from
CC spliceosomes. {ECO:0000269|PubMed:15452114}.
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: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA15715.1; -; Genomic_DNA.
DR PIR; T37496; T37496.
DR RefSeq; NP_593253.1; NM_001018650.2.
DR AlphaFoldDB; O42643; -.
DR SMR; O42643; -.
DR BioGRID; 279416; 24.
DR IntAct; O42643; 4.
DR STRING; 4896.SPAC10F6.02c.1; -.
DR iPTMnet; O42643; -.
DR MaxQB; O42643; -.
DR PaxDb; O42643; -.
DR PRIDE; O42643; -.
DR EnsemblFungi; SPAC10F6.02c.1; SPAC10F6.02c.1:pep; SPAC10F6.02c.
DR GeneID; 2542978; -.
DR KEGG; spo:SPAC10F6.02c; -.
DR PomBase; SPAC10F6.02c; prp22.
DR VEuPathDB; FungiDB:SPAC10F6.02c; -.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_2_3_1; -.
DR InParanoid; O42643; -.
DR OMA; DPMVAPE; -.
DR PhylomeDB; O42643; -.
DR PRO; PR:O42643; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
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; ISS:PomBase.
DR GO; GO:0000390; P:spliceosomal complex disassembly; ISS:PomBase.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR Gene3D; 2.40.50.140; -; 1.
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; IPR044762; DHX8/Prp22_DEXHc.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 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.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1168
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT prp22"
FT /id="PRO_0000055134"
FT DOMAIN 207..280
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 520..684
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 702..882
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 631..634
FT /note="DEAH box"
FT COMPBIAS 82..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533..540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1168 AA; 131492 MW; 42503E03FE59E126 CRC64;
MDDLKELEYL SLVSKVASEI RNHTGIDDNT LAEFIINLHD QSKNYDEFKN NVLSCGGEFT
DSFLQNISRL IKEIKPKDDI PTDNVNNGSN SVNGASHDLD SKDVDKQHQR KMFPGLSIPN
STNNLRDRPA LMDNAMDELE ELSTLAKTRR NDRDSRRDER HYLNGIRERR ERSISPSFSH
HSRTSISGQS HSSRSSRGPL LNAPTLYGIY SGVVSGIKDF GAFVTLDGFR KRTDGLVHIS
NIQLNGRLDH PSEAVSYGQP VFVKVIRIDE SAKRISLSMK EVNQVTGEDL NPDQVSRSTK
KGSGANAIPL SAQNSEIGHV NPLETFTSNG RKRLTSPEIW ELQQLAASGA ISATDIPELN
DGFNTNNAAE INPEDDEDVE IELREEEPGF LAGQTKVSLK LSPIKVVKAP DGSLSRAAMQ
GQILANDRRE IRQKEAKLKS EQEMEKQDLS LSWQDTMSNP QDRKFAQDVR DSAARQLTSE
TPSWRQATRN ANISYGKRTT LSMKEQREGL PVFKLRKQFL EAVSKNQILV LLGETGSGKT
TQITQYLAEE GYTSDSKMIG CTQPRRVAAM SVAKRVAEEV GCRVGEEVGY TIRFEDKTSR
MTQIKYMTDG MLQRECLVDP LLSKYSVIIL DEAHERTVAT DVLFGLLKGT VLKRPDLKLI
VTSATLDAER FSSYFYKCPI FTIPGRSYPV EIMYTKQPEA DYLDAALMTV MQIHLSEGPG
DILVFLTGQE EIDTSCEILY ERSKMLGDSI PELVILPVYS ALPSEIQSRI FEPAPPGGRK
VVIATNIAET SLTIDGIYYV VDPGFVKQSC FDPKLGMDSL IVTPISQAQA RQRSGRAGRT
GPGKCYRLYT ESAYRNEMLP SPIPEIQRQN LSHTILMLKA MGINDLLNFD FMDPPPAQTM
IAALQNLYAL SALDDEGLLT PLGRKMADFP MEPQLSKVLI TSVELGCSEE MLSIIAMLSV
PNIWSRPREK QQEADRQRAQ FANPESDHLT LLNVYTTWKM NRCSDNWCYE HYIQARGMRR
AEDVRKQLIR LMDRYRHPVV SCGRKRELIL RALCSGYFTN VAKRDSHEGC YKTIVENAPV
YMHPSGVLFG KAAEWVIYHE LIQTSKEYMH TVSTVNPKWL VEVAPTFFKF ANANQVSKTK
KNLKVLPLYN RFEKPDEWRI SKQRKGGR
