BRR2_SCHPO
ID BRR2_SCHPO Reviewed; 2176 AA.
AC Q9UT24;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Pre-mRNA-splicing factor brr2;
DE EC=3.6.4.13;
DE AltName: Full=Pre-mRNA-splicing factor spp41;
DE AltName: Full=Pre-mRNA-splicing helicase BRR2;
GN Name=brr2; Synonyms=spp41; ORFNames=SPAC9.03c;
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 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).
RN [3]
RP FUNCTION, INTERACTION WITH PRP1, AND MUTAGENESIS OF ALA-311.
RX PubMed=16133344; DOI=10.1007/s00294-005-0013-6;
RA Bottner C.A., Schmidt H., Vogel S., Michele M., Kaeufer N.F.;
RT "Multiple genetic and biochemical interactions of Brr2, Prp8, Prp31, Prp1
RT and Prp4 kinase suggest a function in the control of the activation of
RT spliceosomes in Schizosaccharomyces pombe.";
RL Curr. Genet. 48:151-161(2005).
RN [4]
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 [5]
RP INTERACTION WITH TLS1.
RX PubMed=25245948; DOI=10.1093/nar/gku842;
RA Wang J., Tadeo X., Hou H., Andrews S., Moresco J.J., Yates J.R. III,
RA Nagy P.L., Jia S.;
RT "Tls1 regulates splicing of shelterin components to control telomeric
RT heterochromatin assembly and telomere length.";
RL Nucleic Acids Res. 42:11419-11432(2014).
CC -!- FUNCTION: Involved in pre-mRNA splicing. May be involved in endoplasmic
CC reticulum-associated protein degradation (ERAD) and required for growth
CC at low and high temperatures (By similarity). Required for pre-
CC spliceosome formation, which is the first step of pre-mRNA splicing.
CC This protein is associated with snRNP U5. Has a role in branch site-3'
CC splice site selection. Associates with the branch site-3' splice 3'-
CC exon region. {ECO:0000250, ECO:0000269|PubMed:16133344}.
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. Interacts with prp1 (PubMed:11884590,
CC PubMed:16133344). Interacts with tls1 (PubMed:25245948).
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:16133344,
CC ECO:0000269|PubMed:25245948}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB57421.1; -; Genomic_DNA.
DR PIR; T39188; T39188.
DR RefSeq; NP_593346.1; NM_001018778.2.
DR AlphaFoldDB; Q9UT24; -.
DR SMR; Q9UT24; -.
DR BioGRID; 280090; 58.
DR IntAct; Q9UT24; 8.
DR STRING; 4896.SPAC9.03c.1; -.
DR iPTMnet; Q9UT24; -.
DR MaxQB; Q9UT24; -.
DR PaxDb; Q9UT24; -.
DR PRIDE; Q9UT24; -.
DR EnsemblFungi; SPAC9.03c.1; SPAC9.03c.1:pep; SPAC9.03c.
DR GeneID; 2543676; -.
DR KEGG; spo:SPAC9.03c; -.
DR PomBase; SPAC9.03c; brr2.
DR VEuPathDB; FungiDB:SPAC9.03c; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; Q9UT24; -.
DR OMA; ESFWIIV; -.
DR PhylomeDB; Q9UT24; -.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:Q9UT24; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:PomBase.
DR GO; GO:0005682; C:U5 snRNP; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0000393; P:spliceosomal conformational changes to generate catalytic conformation; IGI:PomBase.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..2176
FT /note="Pre-mRNA-splicing factor brr2"
FT /id="PRO_0000290645"
FT DOMAIN 529..712
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 723..956
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1019..1324
FT /note="SEC63 1"
FT DOMAIN 1374..1550
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1587..1771
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1848..2162
FT /note="SEC63 2"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 654..657
FT /note="DEAH box"
FT BINDING 542..549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1387..1394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 311
FT /note="A->E: In spp41-1."
FT /evidence="ECO:0000269|PubMed:16133344"
SQ SEQUENCE 2176 AA; 248809 MW; 369A1FA6EA8951AA CRC64;
MSSAHPKGDS KEPPKHGNSK EKPNYGQSQY SYSAMSNLVT QADRRFVSRR DAEPTGEPES
LVNRVSIADM GSRARIEKPS TLPLELTQEV QEVRLPRKDA ESLEIGIRQP EREKRSSAIL
KYFDSFEILK YNPLTDETRE VYDYILSFIQ QYLGDQSPEI LRSAADLIIE LLKDSSLDEQ
GRKKQIEEVL STELPQDRFS QLVNLGNRLT DYTVEQEEEL NEEGVNESGV PVLFNEADEE
EEAVEAMEED EVAEDEDVVL ETSISQEEEK KNIENPDTEV TFISADTKKV TEIPTVHPRE
IDAFWLQREI AKYFADAVVC QEKTNQAFEA LSADYDLGEL ENELMSIFDY EHFYLVQLLT
KNRWTIVSCT MLKRAATDEE RLGVEEQIRA AGRSWILEAL RPGAITIPDD GLNELNNNVV
EKAEPAPVSE IPLSKTLTSH KIVPKHQVDL ENYVFTEGSR LMSNKAVKLP EGSFRRTGKG
YEEIHVPAPN KAVLGADERL VKIKELPEWS HQAFLNTQSL NRIQSHLYPI AFGTDENILL
CAPTGAGKTN VAMLCILNEL QKHLREDLSF NLQNFKIVYI APLKALVQEM VNNFSKRLTP
YNIRVAELTG DSQLTKQQIS ETQIIVTTPE KWDIITRKAN DLSYVNLVRL VIIDEVHLLH
DERGPVLESI VARIFRHQEE TLEQVRLVGL SATLPNYTDV ASFLHVDPKK GLFYFDSTYR
PCPLKQEFIG ITEKTPFKRM QTTNEACYEK VMQHAGKNQV LIFVHSRKET AKTARFIRDK
ALEEETIGHL LRSDAASREI LRAEADSTSD ENLKDLLPYG FAIHHAGMRR EDRQTSEDLF
ADGTIQVLVS TATLAWGVNL PAHTVIIKGT QVYSPEKGIW TELSPQDVLQ MLGRAGRPQF
DTYGEGIIIT AHSELQYYLS LMNQQLPIES QFMRRLADCL NAEVSLGTVR SIEDGVDWLG
YTYLYVRMLR SPALYSVGPE YDDDKYLVQK RADLLHSAAI LLEKCKLLVY NRQSGTLTAT
ELGKVAASYY VTHNSMAIYN RLLMQTTSFI ELFRVFSFSD EFKHIPVREE EKVELAKLLE
RVPIPIRERL DEPAAKINAL LQSYISRQRL DGFALVADMV YVTQSAGRIM RAIFEISLRR
GWSSVATLSL DTCKMIEKRL WPTMSPLRQF PNCPSEVIRR VEKKEFPWQR YFDLDPAELG
ELVGVPKEGR RVYNMVQSFP RLSVEAHVQP ITRSLVRVEL VINSQFNWDD HLSGTSEAFW
ILVEDVDGDR LLHYEQFFLL KKYKDDEHIV NFTVPLLEPL PPCYFIKIVS DRWLHSITKV
PLSFQRLIMP EKFPAPTPLL DLQNAPVSSL NNPSFISLYP NFKFFNKIQT QVFNSVYKTN
DSVFIGAPNG SGKTVCAELA LLHHWSQEDY GTAVYIAPIQ EIVDRRYEEW YGKFSDLGDG
KVLVKLTGER SQDLKLIQVA DLIFCTPSQW DSLSKRWRSM RSIQKVDFYI CDELQLLGGF
YGPLYEIVIS RIRYMAVQLE KNIRVVGLSV SVANARDLGE WLGTSPQCIF NFSPKDRPNP
LTIHLQSFSI THFPSLMLAM SKPIYRSLKN FISQRKSTIV FTPDRKVAKQ LAFDLVTFSM
ADEDEYLFSL MENEAFNKVE DAALQQSLKH GIAYISEITS SNDQNIVQYL YRHGLIKVLI
ASRDVIYSLK AKSNAVIVMG TQYYDGKEHR YIDYPISELL QMLGFTASIG SSELSQVILM
TVTTKKEYYK KFLNEPLPME SHLQVWLHDA FVSEISTQTI ESKQDAVDWL TWSYMYRRLV
ANPAYYGLQD ITHESVSEFL SDLVETTMND LSEARLITVD DEDDSCVALN LAMIASHYGI
TYITMQTFAL SLSERTKMKG LLEIVTSAAE YEQLPIRKYE DIVLERIHSR LPVRLSNPNY
EDPHTKSFIL LAAHFSRFEL PPGLVIDQKF ILTRVHNLLG ACVDTLSSEG HLIACIRPME
MSQMVTQALW DRDSPLKQIP YFDDALIERC NKEGVHDVFD IIDLDDEKRT ELLHMDNAHL
AKCAEFINKY PDIDIDFEIE DSEDVHANSP SVLIVQLTRE LEEDEEVDTT VIAPYFPAQK
TEHWWLVISD DKTLLAIKKI TLGRSLTTKM EFVPPAMGTL KYKLSCFSDS YMGVDYEKEF
ECNVLEPLDT EMEDGE
