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Protein

Pre-mRNA-splicing factor brr2

Gene

brr2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity). Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U5. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region.By similarity1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi542 – 5498ATPPROSITE-ProRule annotation
Nucleotide bindingi1387 – 13948ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • spliceosomal conformational changes to generate catalytic conformation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-72165. mRNA Splicing - Minor Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor brr2 (EC:3.6.4.13)
Alternative name(s):
Pre-mRNA-splicing factor spp41
Pre-mRNA-splicing helicase BRR2
Gene namesi
Name:brr2
Synonyms:spp41
ORF Names:SPAC9.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC9.03c.
PomBaseiSPAC9.03c. brr2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
  • spliceosomal complex Source: PomBase
  • U4/U6 x U5 tri-snRNP complex Source: PomBase
  • U5 snRNP Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi311 – 3111A → E in spp41-1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21762176Pre-mRNA-splicing factor brr2PRO_0000290645Add
BLAST

Proteomic databases

MaxQBiQ9UT24.

Interactioni

Subunit structurei

Belongs to the 40S cdc5-associated complex (or cwf complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5, cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27, cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16, cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26, cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10, prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1, smd1, smd3, smf1, smg1 and syf2. Interacts with prp1.2 Publications

Protein-protein interaction databases

BioGridi280090. 18 interactions.
IntActiQ9UT24. 8 interactions.
MINTiMINT-4709395.

Structurei

3D structure databases

ProteinModelPortaliQ9UT24.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini529 – 712184Helicase ATP-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini723 – 956234Helicase C-terminal 1PROSITE-ProRule annotationAdd
BLAST
Domaini1019 – 1324306SEC63 1Add
BLAST
Domaini1374 – 1550177Helicase ATP-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini1587 – 1771185Helicase C-terminal 2PROSITE-ProRule annotationAdd
BLAST
Domaini1848 – 2162315SEC63 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi654 – 6574DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi215 – 27965Glu-richAdd
BLAST

Sequence similaritiesi

Contains 2 helicase ATP-binding domains.PROSITE-ProRule annotation
Contains 2 helicase C-terminal domains.PROSITE-ProRule annotation
Contains 2 SEC63 domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000157749.
InParanoidiQ9UT24.
KOiK12854.
OMAiPDHHSQF.
OrthoDBiEOG7XDBQ3.
PhylomeDBiQ9UT24.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000008. C2_dom.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 1 hit.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM00487. DEXDc. 2 hits.
SM00490. HELICc. 1 hit.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52540. SSF52540. 4 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UT24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAHPKGDS KEPPKHGNSK EKPNYGQSQY SYSAMSNLVT QADRRFVSRR
60 70 80 90 100
DAEPTGEPES LVNRVSIADM GSRARIEKPS TLPLELTQEV QEVRLPRKDA
110 120 130 140 150
ESLEIGIRQP EREKRSSAIL KYFDSFEILK YNPLTDETRE VYDYILSFIQ
160 170 180 190 200
QYLGDQSPEI LRSAADLIIE LLKDSSLDEQ GRKKQIEEVL STELPQDRFS
210 220 230 240 250
QLVNLGNRLT DYTVEQEEEL NEEGVNESGV PVLFNEADEE EEAVEAMEED
260 270 280 290 300
EVAEDEDVVL ETSISQEEEK KNIENPDTEV TFISADTKKV TEIPTVHPRE
310 320 330 340 350
IDAFWLQREI AKYFADAVVC QEKTNQAFEA LSADYDLGEL ENELMSIFDY
360 370 380 390 400
EHFYLVQLLT KNRWTIVSCT MLKRAATDEE RLGVEEQIRA AGRSWILEAL
410 420 430 440 450
RPGAITIPDD GLNELNNNVV EKAEPAPVSE IPLSKTLTSH KIVPKHQVDL
460 470 480 490 500
ENYVFTEGSR LMSNKAVKLP EGSFRRTGKG YEEIHVPAPN KAVLGADERL
510 520 530 540 550
VKIKELPEWS HQAFLNTQSL NRIQSHLYPI AFGTDENILL CAPTGAGKTN
560 570 580 590 600
VAMLCILNEL QKHLREDLSF NLQNFKIVYI APLKALVQEM VNNFSKRLTP
610 620 630 640 650
YNIRVAELTG DSQLTKQQIS ETQIIVTTPE KWDIITRKAN DLSYVNLVRL
660 670 680 690 700
VIIDEVHLLH DERGPVLESI VARIFRHQEE TLEQVRLVGL SATLPNYTDV
710 720 730 740 750
ASFLHVDPKK GLFYFDSTYR PCPLKQEFIG ITEKTPFKRM QTTNEACYEK
760 770 780 790 800
VMQHAGKNQV LIFVHSRKET AKTARFIRDK ALEEETIGHL LRSDAASREI
810 820 830 840 850
LRAEADSTSD ENLKDLLPYG FAIHHAGMRR EDRQTSEDLF ADGTIQVLVS
860 870 880 890 900
TATLAWGVNL PAHTVIIKGT QVYSPEKGIW TELSPQDVLQ MLGRAGRPQF
910 920 930 940 950
DTYGEGIIIT AHSELQYYLS LMNQQLPIES QFMRRLADCL NAEVSLGTVR
960 970 980 990 1000
SIEDGVDWLG YTYLYVRMLR SPALYSVGPE YDDDKYLVQK RADLLHSAAI
1010 1020 1030 1040 1050
LLEKCKLLVY NRQSGTLTAT ELGKVAASYY VTHNSMAIYN RLLMQTTSFI
1060 1070 1080 1090 1100
ELFRVFSFSD EFKHIPVREE EKVELAKLLE RVPIPIRERL DEPAAKINAL
1110 1120 1130 1140 1150
LQSYISRQRL DGFALVADMV YVTQSAGRIM RAIFEISLRR GWSSVATLSL
1160 1170 1180 1190 1200
DTCKMIEKRL WPTMSPLRQF PNCPSEVIRR VEKKEFPWQR YFDLDPAELG
1210 1220 1230 1240 1250
ELVGVPKEGR RVYNMVQSFP RLSVEAHVQP ITRSLVRVEL VINSQFNWDD
1260 1270 1280 1290 1300
HLSGTSEAFW ILVEDVDGDR LLHYEQFFLL KKYKDDEHIV NFTVPLLEPL
1310 1320 1330 1340 1350
PPCYFIKIVS DRWLHSITKV PLSFQRLIMP EKFPAPTPLL DLQNAPVSSL
1360 1370 1380 1390 1400
NNPSFISLYP NFKFFNKIQT QVFNSVYKTN DSVFIGAPNG SGKTVCAELA
1410 1420 1430 1440 1450
LLHHWSQEDY GTAVYIAPIQ EIVDRRYEEW YGKFSDLGDG KVLVKLTGER
1460 1470 1480 1490 1500
SQDLKLIQVA DLIFCTPSQW DSLSKRWRSM RSIQKVDFYI CDELQLLGGF
1510 1520 1530 1540 1550
YGPLYEIVIS RIRYMAVQLE KNIRVVGLSV SVANARDLGE WLGTSPQCIF
1560 1570 1580 1590 1600
NFSPKDRPNP LTIHLQSFSI THFPSLMLAM SKPIYRSLKN FISQRKSTIV
1610 1620 1630 1640 1650
FTPDRKVAKQ LAFDLVTFSM ADEDEYLFSL MENEAFNKVE DAALQQSLKH
1660 1670 1680 1690 1700
GIAYISEITS SNDQNIVQYL YRHGLIKVLI ASRDVIYSLK AKSNAVIVMG
1710 1720 1730 1740 1750
TQYYDGKEHR YIDYPISELL QMLGFTASIG SSELSQVILM TVTTKKEYYK
1760 1770 1780 1790 1800
KFLNEPLPME SHLQVWLHDA FVSEISTQTI ESKQDAVDWL TWSYMYRRLV
1810 1820 1830 1840 1850
ANPAYYGLQD ITHESVSEFL SDLVETTMND LSEARLITVD DEDDSCVALN
1860 1870 1880 1890 1900
LAMIASHYGI TYITMQTFAL SLSERTKMKG LLEIVTSAAE YEQLPIRKYE
1910 1920 1930 1940 1950
DIVLERIHSR LPVRLSNPNY EDPHTKSFIL LAAHFSRFEL PPGLVIDQKF
1960 1970 1980 1990 2000
ILTRVHNLLG ACVDTLSSEG HLIACIRPME MSQMVTQALW DRDSPLKQIP
2010 2020 2030 2040 2050
YFDDALIERC NKEGVHDVFD IIDLDDEKRT ELLHMDNAHL AKCAEFINKY
2060 2070 2080 2090 2100
PDIDIDFEIE DSEDVHANSP SVLIVQLTRE LEEDEEVDTT VIAPYFPAQK
2110 2120 2130 2140 2150
TEHWWLVISD DKTLLAIKKI TLGRSLTTKM EFVPPAMGTL KYKLSCFSDS
2160 2170
YMGVDYEKEF ECNVLEPLDT EMEDGE
Length:2,176
Mass (Da):248,809
Last modified:May 1, 2000 - v1
Checksum:i369A1FA6EA8951AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB57421.1.
PIRiT39188.
RefSeqiNP_593346.1. NM_001018778.2.

Genome annotation databases

EnsemblFungiiSPAC9.03c.1; SPAC9.03c.1:pep; SPAC9.03c.
GeneIDi2543676.
KEGGispo:SPAC9.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB57421.1.
PIRiT39188.
RefSeqiNP_593346.1. NM_001018778.2.

3D structure databases

ProteinModelPortaliQ9UT24.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280090. 18 interactions.
IntActiQ9UT24. 8 interactions.
MINTiMINT-4709395.

Proteomic databases

MaxQBiQ9UT24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC9.03c.1; SPAC9.03c.1:pep; SPAC9.03c.
GeneIDi2543676.
KEGGispo:SPAC9.03c.

Organism-specific databases

EuPathDBiFungiDB:SPAC9.03c.
PomBaseiSPAC9.03c. brr2.

Phylogenomic databases

HOGENOMiHOG000157749.
InParanoidiQ9UT24.
KOiK12854.
OMAiPDHHSQF.
OrthoDBiEOG7XDBQ3.
PhylomeDBiQ9UT24.

Enzyme and pathway databases

ReactomeiR-SPO-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

NextBioi20804682.
PROiQ9UT24.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.40.50.300. 4 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000008. C2_dom.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR027417. P-loop_NTPase.
IPR004179. Sec63-dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 2 hits.
PF00271. Helicase_C. 1 hit.
PF02889. Sec63. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM00487. DEXDc. 2 hits.
SM00490. HELICc. 1 hit.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52540. SSF52540. 4 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
    Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
    Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CWF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Multiple genetic and biochemical interactions of Brr2, Prp8, Prp31, Prp1 and Prp4 kinase suggest a function in the control of the activation of spliceosomes in Schizosaccharomyces pombe."
    Bottner C.A., Schmidt H., Vogel S., Michele M., Kaeufer N.F.
    Curr. Genet. 48:151-161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRP1, MUTAGENESIS OF ALA-311.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBRR2_SCHPO
AccessioniPrimary (citable) accession number: Q9UT24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.