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Database: UniProt
Entry: O42643
LinkDB: O42643
Original site: O42643 
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   16-OCT-2019, entry version 156.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RT   cerevisiae 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
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS
RP   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
RT   fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel
RT   pre-mRNA 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
CC       distance greater or equal to 15. Mediates the release of the
CC       spliced mRNA from 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
CC       complex), a spliceosome sub-complex reminiscent of a late-stage
CC       spliceosome composed of the U2, U5 and U6 snRNAs and at least
CC       brr2, cdc5, cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2,
CC       spp42/cwf6, cwf7/spf27, cwf8, cwf9, cwf10, cwf11, cwf12,
CC       prp45/cwf13, cwf14, cwf15, cwf16, cwf17, cwf18, cwf19, cwf20,
CC       cwf21, cwf22, cwf23, cwf24, cwf25, cwf26, cyp7/cwf27, cwf28,
CC       cwf29/ist3, lea1, msl1, prp5/cwf1, prp10, prp12/sap130, prp17,
CC       prp22, sap61, sap62, sap114, sap145, slu7, smb1, smd1, smd3, smf1,
CC       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
CC       subfamily. DDX8/PRP22 sub-subfamily. {ECO:0000305}.
DR   EMBL; CU329670; CAA15715.1; -; Genomic_DNA.
DR   PIR; T37496; T37496.
DR   RefSeq; NP_593253.1; NM_001018650.2.
DR   SMR; O42643; -.
DR   BioGrid; 279416; 22.
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   EuPathDB; FungiDB:SPAC10F6.02c; -.
DR   PomBase; SPAC10F6.02c; prp22.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; O42643; -.
DR   KO; K12818; -.
DR   OMA; RIQKAIC; -.
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: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   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
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; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1168       Pre-mRNA-splicing factor ATP-dependent
FT                                RNA helicase prp22.
FT                                /FTId=PRO_0000055134.
FT   DOMAIN      207    280       S1 motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00180}.
FT   DOMAIN      520    684       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      702    882       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     533    540       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       631    634       DEAH box.
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
//
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