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Protein

Pre-mRNA-splicing helicase BRR2

Gene

BRR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi521 – 528ATPPROSITE-ProRule annotation8
Nucleotide bindingi1370 – 1377ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • nucleic acid binding Source: InterPro

GO - Biological processi

  • spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30332-MONOMER.
ReactomeiR-SCE-72165. mRNA Splicing - Minor Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing helicase BRR2 (EC:3.6.4.13)
Alternative name(s):
Protein Snu246
Gene namesi
Name:BRR2
Synonyms:RSS1, SNU246
Ordered Locus Names:YER172C
ORF Names:SYGP-ORF66
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER172C.
SGDiS000000974. BRR2.

Subcellular locationi

GO - Cellular componenti

  • spliceosomal complex Source: UniProtKB-KW
  • U4/U6 x U5 tri-snRNP complex Source: SGD
  • U5 snRNP Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi858G → R: Reduces spliceosomal pre-mRNA splicing. 1 Publication1
Mutagenesisi938W → Q: Strongly reduced unwinding of U4/U6 snRNA. 1 Publication1
Mutagenesisi1107R → A: Reduced ATP-dependent RNA helicase activity. 1 Publication1
Mutagenesisi1110R → N: Abolishes unwinding of U4/U6 snRNA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001020861 – 2163Pre-mRNA-splicing helicase BRR2Add BLAST2163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei403PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32639.
PRIDEiP32639.

PTM databases

iPTMnetiP32639.

Interactioni

Subunit structurei

Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. Interaction with PRP8 is important for recruitment to the U4/U6-U5 tri-snRNP complex. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.6 Publications

Protein-protein interaction databases

BioGridi36925. 160 interactors.
DIPiDIP-850N.
IntActiP32639. 67 interactors.
MINTiMINT-606933.

Structurei

Secondary structure

12163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi114 – 130Combined sources17
Beta strandi133 – 135Combined sources3
Helixi137 – 149Combined sources13
Turni153 – 155Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi161 – 163Combined sources3
Helixi164 – 169Combined sources6
Helixi176 – 186Combined sources11
Beta strandi263 – 265Combined sources3
Turni285 – 287Combined sources3
Helixi292 – 300Combined sources9
Helixi306 – 319Combined sources14
Turni320 – 323Combined sources4
Helixi330 – 338Combined sources9
Turni344 – 346Combined sources3
Helixi347 – 350Combined sources4
Helixi353 – 358Combined sources6
Turni362 – 364Combined sources3
Helixi370 – 377Combined sources8
Turni378 – 380Combined sources3
Turni382 – 387Combined sources6
Helixi388 – 392Combined sources5
Helixi429 – 432Combined sources4
Beta strandi453 – 456Combined sources4
Beta strandi458 – 465Combined sources8
Helixi480 – 482Combined sources3
Helixi485 – 490Combined sources6
Turni493 – 495Combined sources3
Helixi501 – 511Combined sources11
Beta strandi517 – 521Combined sources5
Beta strandi523 – 525Combined sources3
Helixi527 – 540Combined sources14
Beta strandi545 – 550Combined sources6
Beta strandi556 – 560Combined sources5
Helixi564 – 577Combined sources14
Turni579 – 582Combined sources4
Beta strandi585 – 587Combined sources3
Beta strandi591 – 593Combined sources3
Helixi596 – 601Combined sources6
Beta strandi603 – 607Combined sources5
Helixi609 – 617Combined sources9
Helixi619 – 621Combined sources3
Helixi622 – 625Combined sources4
Beta strandi628 – 633Combined sources6
Helixi636 – 640Combined sources5
Helixi644 – 656Combined sources13
Beta strandi659 – 662Combined sources4
Beta strandi666 – 673Combined sources8
Helixi677 – 683Combined sources7
Helixi688 – 690Combined sources3
Beta strandi691 – 693Combined sources3
Helixi696 – 698Combined sources3
Beta strandi699 – 701Combined sources3
Beta strandi703 – 710Combined sources8
Helixi715 – 735Combined sources21
Beta strandi740 – 743Combined sources4
Helixi747 – 762Combined sources16
Turni767 – 770Combined sources4
Helixi776 – 785Combined sources10
Helixi791 – 798Combined sources8
Beta strandi801 – 804Combined sources4
Beta strandi806 – 808Combined sources3
Helixi810 – 821Combined sources12
Beta strandi826 – 830Combined sources5
Helixi833 – 836Combined sources4
Beta strandi842 – 848Combined sources7
Beta strandi851 – 854Combined sources4
Helixi855 – 857Combined sources3
Beta strandi859 – 862Combined sources4
Helixi865 – 873Combined sources9
Beta strandi874 – 876Combined sources3
Turni878 – 880Combined sources3
Beta strandi882 – 891Combined sources10
Helixi892 – 894Combined sources3
Helixi895 – 901Combined sources7
Turni902 – 904Combined sources3
Helixi912 – 915Combined sources4
Helixi916 – 925Combined sources10
Helixi932 – 939Combined sources8
Helixi943 – 950Combined sources8
Turni952 – 956Combined sources5
Helixi960 – 963Combined sources4
Turni964 – 966Combined sources3
Helixi967 – 983Combined sources17
Beta strandi986 – 990Combined sources5
Turni991 – 994Combined sources4
Beta strandi995 – 999Combined sources5
Helixi1000 – 1008Combined sources9
Helixi1012 – 1021Combined sources10
Helixi1028 – 1036Combined sources9
Helixi1039 – 1041Combined sources3
Turni1048 – 1050Combined sources3
Helixi1051 – 1059Combined sources9
Beta strandi1069 – 1071Combined sources3
Helixi1072 – 1084Combined sources13
Helixi1092 – 1119Combined sources28
Helixi1122 – 1137Combined sources16
Beta strandi1141 – 1143Combined sources3
Helixi1145 – 1148Combined sources4
Helixi1154 – 1163Combined sources10
Helixi1168 – 1171Combined sources4
Helixi1178 – 1182Combined sources5
Turni1186 – 1190Combined sources5
Helixi1191 – 1196Combined sources6
Beta strandi1202 – 1224Combined sources23
Helixi1230 – 1233Combined sources4
Beta strandi1237 – 1244Combined sources8
Beta strandi1246 – 1248Combined sources3
Beta strandi1250 – 1259Combined sources10
Beta strandi1261 – 1263Combined sources3
Beta strandi1266 – 1275Combined sources10
Helixi1278 – 1282Combined sources5
Beta strandi1286 – 1297Combined sources12
Beta strandi1301 – 1307Combined sources7
Helixi1331 – 1333Combined sources3
Helixi1337 – 1340Combined sources4
Helixi1350 – 1354Combined sources5
Helixi1356 – 1360Combined sources5
Beta strandi1366 – 1369Combined sources4
Helixi1376 – 1389Combined sources14
Beta strandi1395 – 1398Combined sources4
Helixi1402 – 1416Combined sources15
Turni1417 – 1421Combined sources5
Beta strandi1424 – 1426Combined sources3
Helixi1432 – 1441Combined sources10
Beta strandi1443 – 1447Combined sources5
Helixi1449 – 1455Combined sources7
Helixi1456 – 1461Combined sources6
Helixi1463 – 1466Combined sources4
Beta strandi1470 – 1474Combined sources5
Helixi1476 – 1480Combined sources5
Helixi1482 – 1502Combined sources21
Beta strandi1507 – 1513Combined sources7
Helixi1519 – 1525Combined sources7
Helixi1529 – 1531Combined sources3
Beta strandi1532 – 1534Combined sources3
Helixi1537 – 1539Combined sources3
Beta strandi1544 – 1553Combined sources10
Helixi1561 – 1576Combined sources16
Beta strandi1581 – 1587Combined sources7
Helixi1588 – 1603Combined sources16
Turni1604 – 1606Combined sources3
Helixi1614 – 1622Combined sources9
Helixi1627 – 1629Combined sources3
Helixi1630 – 1634Combined sources5
Beta strandi1637 – 1640Combined sources4
Beta strandi1642 – 1644Combined sources3
Helixi1646 – 1657Combined sources12
Beta strandi1660 – 1667Combined sources8
Helixi1668 – 1670Combined sources3
Beta strandi1671 – 1673Combined sources3
Beta strandi1677 – 1683Combined sources7
Beta strandi1686 – 1689Combined sources4
Turni1690 – 1693Combined sources4
Beta strandi1694 – 1697Combined sources4
Helixi1700 – 1707Combined sources8
Beta strandi1714 – 1716Combined sources3
Beta strandi1718 – 1725Combined sources8
Helixi1726 – 1737Combined sources12
Helixi1746 – 1749Combined sources4
Helixi1750 – 1759Combined sources10
Helixi1766 – 1773Combined sources8
Helixi1777 – 1782Combined sources6
Helixi1786 – 1789Combined sources4
Helixi1796 – 1816Combined sources21
Beta strandi1819 – 1823Combined sources5
Beta strandi1843 – 1846Combined sources4
Beta strandi1847 – 1849Combined sources3
Helixi1860 – 1869Combined sources10
Helixi1876 – 1884Combined sources9
Helixi1887 – 1891Combined sources5
Helixi1898 – 1906Combined sources9
Beta strandi1909 – 1911Combined sources3
Beta strandi1915 – 1917Combined sources3
Beta strandi1919 – 1921Combined sources3
Helixi1922 – 1935Combined sources14
Helixi1941 – 1967Combined sources27
Helixi1973 – 1985Combined sources13
Beta strandi1989 – 1991Combined sources3
Helixi1993 – 1996Combined sources4
Helixi2002 – 2010Combined sources9
Helixi2016 – 2021Combined sources6
Helixi2024 – 2030Combined sources7
Helixi2035 – 2047Combined sources13
Beta strandi2051 – 2057Combined sources7
Helixi2060 – 2062Combined sources3
Beta strandi2067 – 2079Combined sources13
Beta strandi2099 – 2105Combined sources7
Helixi2106 – 2108Combined sources3
Beta strandi2110 – 2117Combined sources8
Beta strandi2121 – 2131Combined sources11
Beta strandi2135 – 2148Combined sources14
Beta strandi2154 – 2163Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HIBX-ray2.00A1851-2163[»]
3IM1X-ray1.65A1839-2163[»]
3IM2X-ray1.99A1839-2163[»]
3JCMelectron microscopy3.80N1-2163[»]
4BGDX-ray3.10A442-2163[»]
5DCAX-ray2.80A113-2163[»]
5GANelectron microscopy3.60B1-2163[»]
5GAOelectron microscopy3.60B1-2163[»]
5GAPelectron microscopy3.60B1-2163[»]
5GM6electron microscopy3.50B1-2163[»]
5LJ5electron microscopy3.80B1-2163[»]
5LQWelectron microscopy5.80C1-2163[»]
ProteinModelPortaliP32639.
SMRiP32639.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32639.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini508 – 692Helicase ATP-binding 1PROSITE-ProRule annotationAdd BLAST185
Domaini718 – 921Helicase C-terminalPROSITE-ProRule annotationAdd BLAST204
Domaini998 – 1308SEC63 1Add BLAST311
Domaini1357 – 1533Helicase ATP-binding 2PROSITE-ProRule annotationAdd BLAST177
Domaini1846 – 2160SEC63 2Add BLAST315

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi634 – 637DEIH box4
Motifi1474 – 1477DDAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1570 – 1575Poly-Ala6

Domaini

Contains two helicase domains. The N-terminal helicase domain has catalytic activity by itself, contrary to the C-terminal helicase domain that may have a regulatory role and enhance the activity of the first helicase domain.1 Publication

Sequence similaritiesi

Belongs to the helicase family. SKI2 subfamily.Curated
Contains 2 helicase ATP-binding domains.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 SEC63 domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00860000134500.
HOGENOMiHOG000157749.
InParanoidiP32639.
KOiK12854.
OMAiQVREFQR.
OrthoDBiEOG092C01UD.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR000008. 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]
SMARTiSM00487. DEXDc. 2 hits.
SM00490. HELICc. 1 hit.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
SSF52540. SSF52540. 5 hits.
SSF81296. SSF81296. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEHETKDKA KKIREIYRYD EMSNKVLKVD KRFMNTSQNP QRDAEISQPK
60 70 80 90 100
SMSGRISAKD MGQGLCNNIN KGLKENDVAV EKTGKSASLK KIQQHNTILN
110 120 130 140 150
SSSDFRLHYY PKDPSNVETY EQILQWVTEV LGNDIPHDLI IGTADIFIRQ
160 170 180 190 200
LKENEENEDG NIEERKEKIQ HELGINIDSL KFNELVKLMK NITDYETHPD
210 220 230 240 250
NSNKQAVAIL ADDEKSDEEE VTEMSNNANV LGGEINDNED DDEEYDYNDV
260 270 280 290 300
EVNSKKKNKR ALPNIENDII KLSDSKTSNI ESVPIYSIDE FFLQRKLRSE
310 320 330 340 350
LGYKDTSVIQ DLSEKILNDI ETLEHNPVAL EQKLVDLLKF ENISLAEFIL
360 370 380 390 400
KNRSTIFWGI RLAKSTENEI PNLIEKMVAK GLNDLVEQYK FRETTHSKRE
410 420 430 440 450
LDSGDDQPQS SEAKRTKFSN PAIPPVIDLE KIKFDESSKL MTVTKVSLPE
460 470 480 490 500
GSFKRVKPQY DEIHIPAPSK PVIDYELKEI TSLPDWCQEA FPSSETTSLN
510 520 530 540 550
PIQSKVFHAA FEGDSNMLIC APTGSGKTNI ALLTVLKALS HHYNPKTKKL
560 570 580 590 600
NLSAFKIVYI APLKALVQEQ VREFQRRLAF LGIKVAELTG DSRLSRKQID
610 620 630 640 650
ETQVLVSTPE KWDITTRNSN NLAIVELVRL LIIDEIHLLH DDRGPVLESI
660 670 680 690 700
VARTFWASKY GQEYPRIIGL SATLPNYEDV GRFLRVPKEG LFYFDSSFRP
710 720 730 740 750
CPLSQQFCGI KERNSLKKLK AMNDACYEKV LESINEGNQI IVFVHSRKET
760 770 780 790 800
SRTATWLKNK FAEENITHKL TKNDAGSKQI LKTEAANVLD PSLRKLIESG
810 820 830 840 850
IGTHHAGLTR SDRSLSEDLF ADGLLQVLVC TATLAWGVNL PAHTVIIKGT
860 870 880 890 900
DVYSPEKGSW EQLSPQDVLQ MLGRAGRPRY DTFGEGIIIT DQSNVQYYLS
910 920 930 940 950
VLNQQLPIES QFVSKLVDNL NAEVVAGNIK CRNDAVNWLA YTYLYVRMLA
960 970 980 990 1000
SPMLYKVPDI SSDGQLKKFR ESLVHSALCI LKEQELVLYD AENDVIEATD
1010 1020 1030 1040 1050
LGNIASSFYI NHASMDVYNR ELDEHTTQID LFRIFSMSEE FKYVSVRYEE
1060 1070 1080 1090 1100
KRELKQLLEK APIPIREDID DPLAKVNVLL QSYFSQLKFE GFALNSDIVF
1110 1120 1130 1140 1150
IHQNAGRLLR AMFEICLKRG WGHPTRMLLN LCKSATTKMW PTNCPLRQFK
1160 1170 1180 1190 1200
TCPVEVIKRL EASTVPWGDY LQLETPAEVG RAIRSEKYGK QVYDLLKRFP
1210 1220 1230 1240 1250
KMSVTCNAQP ITRSVMRFNI EIIADWIWDM NVHGSLEPFL LMLEDTDGDS
1260 1270 1280 1290 1300
ILYYDVLFIT PDIVGHEFTL SFTYELKQHN QNNLPPNFFL TLISENWWHS
1310 1320 1330 1340 1350
EFEIPVSFNG FKLPKKFPPP TPLLENISIS TSELGNDDFS EVFEFKTFNK
1360 1370 1380 1390 1400
IQSQVFESLY NSNDSVFVGS GKGTGKTAMA ELALLNHWRQ NKGRAVYINP
1410 1420 1430 1440 1450
SGEKIDFLLS DWNKRFSHLA GGKIINKLGN DPSLNLKLLA KSHVLLATPV
1460 1470 1480 1490 1500
QFELLSRRWR QRKNIQSLEL MIYDDAHEIS QGVYGAVYET LISRMIFIAT
1510 1520 1530 1540 1550
QLEKKIRFVC LSNCLANARD FGEWAGMTKS NIYNFSPSER IEPLEINIQS
1560 1570 1580 1590 1600
FKDVEHISFN FSMLQMAFEA SAAAAGNRNS SSVFLPSRKD CMEVASAFMK
1610 1620 1630 1640 1650
FSKAIEWDML NVEEEQIVPY IEKLTDGHLR APLKHGVGIL YKGMASNDER
1660 1670 1680 1690 1700
IVKRLYEYGA VSVLLISKDC SAFACKTDEV IILGTNLYDG AEHKYMPYTI
1710 1720 1730 1740 1750
NELLEMVGLA SGNDSMAGKV LILTSHNMKA YYKKFLIEPL PTESYLQYII
1760 1770 1780 1790 1800
HDTLNNEIAN SIIQSKQDCV DWFTYSYFYR RIHVNPSYYG VRDTSPHGIS
1810 1820 1830 1840 1850
VFLSNLVETC LNDLVESSFI EIDDTEAEVT AEVNGGDDEA TEIISTLSNG
1860 1870 1880 1890 1900
LIASHYGVSF FTIQSFVSSL SNTSTLKNML YVLSTAVEFE SVPLRKGDRA
1910 1920 1930 1940 1950
LLVKLSKRLP LRFPEHTSSG SVSFKVFLLL QAYFSRLELP VDFQNDLKDI
1960 1970 1980 1990 2000
LEKVVPLINV VVDILSANGY LNATTAMDLA QMLIQGVWDV DNPLRQIPHF
2010 2020 2030 2040 2050
NNKILEKCKE INVETVYDIM ALEDEERDEI LTLTDSQLAQ VAAFVNNYPN
2060 2070 2080 2090 2100
VELTYSLNNS DSLISGVKQK ITIQLTRDVE PENLQVTSEK YPFDKLESWW
2110 2120 2130 2140 2150
LVLGEVSKKE LYAIKKVTLN KETQQYELEF DTPTSGKHNL TIWCVCDSYL
2160
DADKELSFEI NVK
Length:2,163
Mass (Da):246,185
Last modified:February 1, 1995 - v2
Checksum:iDFAF7E3B7168D944
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18922 Genomic DNA. Translation: AAB64699.1.
BK006939 Genomic DNA. Translation: DAA07834.1.
PIRiS50675.
RefSeqiNP_011099.1. NM_001179062.1.

Genome annotation databases

EnsemblFungiiYER172C; YER172C; YER172C.
GeneIDi856919.
KEGGisce:YER172C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18922 Genomic DNA. Translation: AAB64699.1.
BK006939 Genomic DNA. Translation: DAA07834.1.
PIRiS50675.
RefSeqiNP_011099.1. NM_001179062.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HIBX-ray2.00A1851-2163[»]
3IM1X-ray1.65A1839-2163[»]
3IM2X-ray1.99A1839-2163[»]
3JCMelectron microscopy3.80N1-2163[»]
4BGDX-ray3.10A442-2163[»]
5DCAX-ray2.80A113-2163[»]
5GANelectron microscopy3.60B1-2163[»]
5GAOelectron microscopy3.60B1-2163[»]
5GAPelectron microscopy3.60B1-2163[»]
5GM6electron microscopy3.50B1-2163[»]
5LJ5electron microscopy3.80B1-2163[»]
5LQWelectron microscopy5.80C1-2163[»]
ProteinModelPortaliP32639.
SMRiP32639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36925. 160 interactors.
DIPiDIP-850N.
IntActiP32639. 67 interactors.
MINTiMINT-606933.

PTM databases

iPTMnetiP32639.

Proteomic databases

MaxQBiP32639.
PRIDEiP32639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER172C; YER172C; YER172C.
GeneIDi856919.
KEGGisce:YER172C.

Organism-specific databases

EuPathDBiFungiDB:YER172C.
SGDiS000000974. BRR2.

Phylogenomic databases

GeneTreeiENSGT00860000134500.
HOGENOMiHOG000157749.
InParanoidiP32639.
KOiK12854.
OMAiQVREFQR.
OrthoDBiEOG092C01UD.

Enzyme and pathway databases

BioCyciYEAST:G3O-30332-MONOMER.
ReactomeiR-SCE-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

EvolutionaryTraceiP32639.
PROiP32639.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR000008. 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]
SMARTiSM00487. DEXDc. 2 hits.
SM00490. HELICc. 1 hit.
SM00973. Sec63. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
SSF52540. SSF52540. 5 hits.
SSF81296. SSF81296. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 2 hits.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBRR2_YEAST
AccessioniPrimary (citable) accession number: P32639
Secondary accession number(s): D3DM80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1440 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

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.