PRP8_YEAST
ID PRP8_YEAST Reviewed; 2413 AA.
AC P33334; D3DLB4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Pre-mRNA-splicing factor 8;
GN Name=PRP8; Synonyms=DBF3, DNA39, RNA8, SLT21, USA2;
GN OrderedLocusNames=YHR165C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7785334; DOI=10.1002/yea.320110406;
RA Hodges P.E., Jackson S.P., Brown J.D., Beggs J.D.;
RT "Extraordinary sequence conservation of the PRP8 splicing factor.";
RL Yeast 11:337-342(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7838707; DOI=10.1093/nar/22.25.5555;
RA Shea J.E., Toyn J.H., Johnston L.H.;
RT "The budding yeast U5 snRNP Prp8 is a highly conserved protein which links
RT RNA splicing with cell cycle progression.";
RL Nucleic Acids Res. 22:5555-5564(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2835658; DOI=10.1128/mcb.8.3.1067-1075.1988;
RA Jackson S.P., Lossky M., Beggs J.D.;
RT "Cloning of the RNA8 gene of Saccharomyces cerevisiae, detection of the
RT RNA8 protein, and demonstration that it is essential for nuclear pre-mRNA
RT splicing.";
RL Mol. Cell. Biol. 8:1067-1075(1988).
RN [6]
RP FUNCTION, AND INTERACTION WITH PRP40.
RX PubMed=9150140; DOI=10.1016/s0092-8674(00)80221-4;
RA Abovich N., Rosbash M.;
RT "Cross-intron bridging interactions in the yeast commitment complex are
RT conserved in mammals.";
RL Cell 89:403-412(1997).
RN [7]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA Fabrizio P.;
RT "Identification by mass spectrometry and functional analysis of novel
RT proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL EMBO J. 18:4535-4548(1999).
RN [8]
RP FUNCTION.
RX PubMed=10444596; DOI=10.1101/gad.13.15.1983;
RA Siatecka M., Reyes J.L., Konarska M.M.;
RT "Functional interactions of Prp8 with both splice sites at the spliceosomal
RT catalytic center.";
RL Genes Dev. 13:1983-1993(1999).
RN [9]
RP INTERACTION WITH SNP1.
RX PubMed=11425851; DOI=10.1074/jbc.m100022200;
RA Awasthi S., Palmer R., Castro M., Mobarak C.D., Ruby S.W.;
RT "New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA splicing.";
RL J. Biol. Chem. 276:31004-31015(2001).
RN [10]
RP IDENTIFICATION IN THE CWC 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [12]
RP FUNCTION.
RX PubMed=12773561; DOI=10.1128/mcb.23.12.4174-4186.2003;
RA McPheeters D.S., Muhlenkamp P.;
RT "Spatial organization of protein-RNA interactions in the branch site-3'
RT splice site region during pre-mRNA splicing in yeast.";
RL Mol. Cell. Biol. 23:4174-4186(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17934474; DOI=10.1038/nsmb1303;
RA Boon K.L., Grainger R.J., Ehsani P., Barrass J.D., Auchynnikava T.,
RA Inglehearn C.F., Beggs J.D.;
RT "prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP
RT maturation defect in yeast.";
RL Nat. Struct. Mol. Biol. 14:1077-1083(2007).
RN [15]
RP MUTAGENESIS OF ASP-1853 AND ASP-1854, AND LACK OF METAL-BINDING SITE.
RX PubMed=18836455; DOI=10.1038/nsmb.1505;
RA Ritchie D.B., Schellenberg M.J., Gesner E.M., Raithatha S.A., Stuart D.T.,
RA Macmillan A.M.;
RT "Structural elucidation of a PRP8 core domain from the heart of the
RT spliceosome.";
RL Nat. Struct. Mol. Biol. 15:1199-1205(2008).
RN [16]
RP SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND ELECTRON
RP MICROSCOPY.
RX PubMed=18953335; DOI=10.1038/nsmb.1506;
RA Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B.,
RA Stark H., Fabrizio P., Luhrmann R.;
RT "Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-
RT snRNP by electron microscopy.";
RL Nat. Struct. Mol. Biol. 15:1206-1212(2008).
RN [17]
RP FUNCTION, AND INTERACTION WITH BRR2.
RX PubMed=19098916; DOI=10.1038/nsmb.1535;
RA Maeder C., Kutach A.K., Guthrie C.;
RT "ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the
RT C terminus of Prp8.";
RL Nat. Struct. Mol. Biol. 16:42-48(2009).
RN [18]
RP INTERACTION WITH CWC21 AND SNU114.
RX PubMed=19854871; DOI=10.1261/rna.1908309;
RA Grainger R.J., Barrass J.D., Jacquier A., Rain J.-C., Beggs J.D.;
RT "Physical and genetic interactions of yeast Cwc21p, an ortholog of human
RT SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome.";
RL RNA 15:2161-2173(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2147-2413, AND LACK OF METAL
RP BINDING.
RX PubMed=17317632; DOI=10.1016/j.molcel.2007.01.023;
RA Pena V., Liu S., Bujnicki J.M., Luehrmann R., Wahl M.C.;
RT "Structure of a multipartite protein-protein interaction domain in splicing
RT factor Prp8 and its link to retinitis pigmentosa.";
RL Mol. Cell 25:615-624(2007).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1827-2092, LACK OF METAL BINDING,
RP DOMAIN, AND MUTAGENESIS OF ASP-1853; ASP-1854; THR-1855; THR-1936 AND
RP ARG-1937.
RX PubMed=18843295; DOI=10.1038/emboj.2008.209;
RA Pena V., Rozov A., Fabrizio P., Luehrmann R., Wahl M.C.;
RT "Structure and function of an RNase H domain at the heart of the
RT spliceosome.";
RL EMBO J. 27:2929-2940(2008).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1822-2095, LACK OF METAL BINDING,
RP FUNCTION, AND MUTAGENESIS OF ASP-1853.
RX PubMed=18779563; DOI=10.1073/pnas.0805960105;
RA Yang K., Zhang L., Xu T., Heroux A., Zhao R.;
RT "Crystal structure of the beta-finger domain of Prp8 reveals analogy to
RT ribosomal proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13817-13822(2008).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1836-2092 IN COMPLEX WITH AAR2,
RP AND INTERACTION WITH AAR2.
RX PubMed=21764848; DOI=10.1101/gad.635911;
RA Weber G., Cristao V.F., de Lima Alves F., Santos K.F., Holton N.,
RA Rappsilber J., Beggs J.D., Wahl M.C.;
RT "Mechanism for Aar2p function as a U5 snRNP assembly factor.";
RL Genes Dev. 25:1601-1612(2011).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 885-2413 IN COMPLEX WITH AAR2,
RP FUNCTION, DOMAIN, INTERACTION WITH AAR2, AND MUTAGENESIS OF HIS-1658;
RP GLU-1684; HIS-1687; ASP-1700 AND ASP-1735.
RX PubMed=23354046; DOI=10.1038/nature11843;
RA Galej W.P., Oubridge C., Newman A.J., Nagai K.;
RT "Crystal structure of Prp8 reveals active site cavity of the spliceosome.";
RL Nature 493:638-643(2013).
CC -!- FUNCTION: Functions as a scaffold that mediates the ordered assembly of
CC spliceosomal proteins and snRNAs. Required for association of BRR2 with
CC the spliceosomal U5 snRNP, and the subsequent assembly of the U4/U6-U5
CC tri-snRNP complex. Functions as scaffold that positions spliceosomal
CC U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that
CC splicing can occur. Interacts with both the 5' and the 3' splice site,
CC as well as the branch region. Has a role in branch site-3' splice site
CC selection. Associates with the branch site-3' splice 3'-exon region.
CC Also has a role in cell cycle. {ECO:0000269|PubMed:10444596,
CC ECO:0000269|PubMed:12773561, ECO:0000269|PubMed:17934474,
CC ECO:0000269|PubMed:18779563, ECO:0000269|PubMed:19098916,
CC ECO:0000269|PubMed:23354046, ECO:0000269|PubMed:2835658,
CC ECO:0000269|PubMed:9150140}.
CC -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31,
CC PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC Belongs to the CWC complex (or CEF1-associated complex), a spliceosome
CC sub-complex reminiscent of a late-stage spliceosome composed of the U2,
CC U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1,
CC CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2,
CC HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21,
CC PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309,
CC SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with PRP40 and SNP1.
CC Interacts (via SCwid domain) with CWC21. Interacts (via SCwid domain)
CC with SNU114 (via N-terminus). Interacts (via RNase H homology domain
CC and MPN domain) with BRR2; this modulates BRR2 ATPase and helicase
CC activity. Interacts (via RNase H homology domain) with AAR2. AAR2 and
CC BRR2 compete for PRP8 binding, and during U5 snRNP maturation BRR2
CC displaces the initially bound AAR2. Is associated with snRNP U5,
CC together with SNU114 and BRR2. {ECO:0000269|PubMed:10449419,
CC ECO:0000269|PubMed:11425851, ECO:0000269|PubMed:11884590,
CC ECO:0000269|PubMed:17934474, ECO:0000269|PubMed:18953335,
CC ECO:0000269|PubMed:19098916, ECO:0000269|PubMed:19854871,
CC ECO:0000269|PubMed:21764848, ECO:0000269|PubMed:23354046,
CC ECO:0000269|PubMed:9150140}.
CC -!- INTERACTION:
CC P33334; P32357: AAR2; NbExp=11; IntAct=EBI-465, EBI-340;
CC P33334; P32639: BRR2; NbExp=25; IntAct=EBI-465, EBI-861;
CC P33334; P36006: MYO3; NbExp=4; IntAct=EBI-465, EBI-11670;
CC P33334; Q04439: MYO5; NbExp=4; IntAct=EBI-465, EBI-11687;
CC P33334; Q00916: SNP1; NbExp=3; IntAct=EBI-465, EBI-724;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17934474,
CC ECO:0000269|PubMed:2835658}.
CC -!- DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with
CC deubiquitinating enzymes, but lacks the residues that would bind the
CC catalytic metal ion.
CC -!- DOMAIN: Contains a region with structural similarity to reverse
CC transcripase, presenting the classical thumb, fingers and palm
CC architecture, but lacks enzyme activity, since the essential metal-
CC binding residues are not conserved.
CC -!- DOMAIN: Contains a region with structural similarity to type-2
CC restriction endonucleases, but the residues that would bind catalytic
CC metal ions in endonucleases are instead involved in hydrogen bonds that
CC stabilize a highly conserved loop.
CC -!- DOMAIN: Contains a region with structural similarity to RNase H, but
CC lacks RNase H activity.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z24732; CAA80854.1; -; Genomic_DNA.
DR EMBL; L29421; AAA67044.1; -; Genomic_DNA.
DR EMBL; U00027; AAB68011.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06858.1; -; Genomic_DNA.
DR PIR; S34670; S34670.
DR RefSeq; NP_012035.1; NM_001179296.1.
DR PDB; 2OG4; X-ray; 2.00 A; A=2147-2397.
DR PDB; 3E66; X-ray; 2.05 A; A/B=1822-2095.
DR PDB; 3E9O; X-ray; 2.00 A; A=1836-2087.
DR PDB; 3E9P; X-ray; 2.10 A; A/B=1833-2087.
DR PDB; 3JCM; EM; 3.80 A; A=1-2413.
DR PDB; 3SBG; X-ray; 3.28 A; A=1836-2397.
DR PDB; 3SBT; X-ray; 1.80 A; A=1836-2092.
DR PDB; 3ZEF; X-ray; 3.10 A; B/E=885-2413.
DR PDB; 4BGD; X-ray; 3.10 A; C=2148-2395.
DR PDB; 4I43; X-ray; 2.00 A; B=885-2413.
DR PDB; 4ILG; X-ray; 2.10 A; B=1836-2090, C=2147-2413.
DR PDB; 4ILH; X-ray; 1.85 A; A=1836-2090.
DR PDB; 4ILJ; X-ray; 2.00 A; A/B=1836-2090.
DR PDB; 5DCA; X-ray; 2.80 A; J=2148-2398.
DR PDB; 5GAM; EM; 3.70 A; A=1-735.
DR PDB; 5GAN; EM; 3.60 A; A=1-2413.
DR PDB; 5GAO; EM; 3.60 A; A=2147-2413.
DR PDB; 5GAP; EM; 3.60 A; A=1-2413.
DR PDB; 5GM6; EM; 3.50 A; A=128-2413.
DR PDB; 5GMK; EM; 3.40 A; A=1-2413.
DR PDB; 5LJ3; EM; 3.80 A; A=1-2413.
DR PDB; 5LJ5; EM; 3.80 A; A=1-2413.
DR PDB; 5LQW; EM; 5.80 A; A=1-2413.
DR PDB; 5M52; X-ray; 3.40 A; C/D=2147-2413.
DR PDB; 5M5P; X-ray; 4.20 A; B/D=2147-2413.
DR PDB; 5MPS; EM; 3.85 A; A=1-2413.
DR PDB; 5MQ0; EM; 4.17 A; A=1-2413.
DR PDB; 5NRL; EM; 7.20 A; A=1-2413.
DR PDB; 5QY1; X-ray; 1.72 A; A=1836-2090.
DR PDB; 5QY2; X-ray; 1.36 A; A=1836-2090.
DR PDB; 5QY3; X-ray; 1.58 A; A=1836-2090.
DR PDB; 5QY4; X-ray; 1.57 A; A=1836-2090.
DR PDB; 5QY5; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QY6; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QY7; X-ray; 1.67 A; A=1836-2090.
DR PDB; 5QY8; X-ray; 1.59 A; A=1836-2090.
DR PDB; 5QY9; X-ray; 1.40 A; A=1836-2090.
DR PDB; 5QYA; X-ray; 1.55 A; A=1836-2090.
DR PDB; 5QYB; X-ray; 2.10 A; A=1836-2090.
DR PDB; 5QYC; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5QYD; X-ray; 1.67 A; A=1836-2090.
DR PDB; 5QYE; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QYF; X-ray; 1.49 A; A=1836-2090.
DR PDB; 5QYG; X-ray; 1.67 A; A=1836-2090.
DR PDB; 5QYH; X-ray; 1.47 A; A=1836-2090.
DR PDB; 5QYI; X-ray; 1.58 A; A=1836-2090.
DR PDB; 5QYJ; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QYK; X-ray; 1.63 A; A=1836-2090.
DR PDB; 5QYL; X-ray; 1.56 A; A=1836-2090.
DR PDB; 5QYM; X-ray; 1.47 A; A=1836-2090.
DR PDB; 5QYN; X-ray; 1.65 A; A=1836-2090.
DR PDB; 5QYO; X-ray; 1.58 A; A=1836-2090.
DR PDB; 5QYP; X-ray; 1.61 A; A=1836-2090.
DR PDB; 5QYQ; X-ray; 1.67 A; A=1836-2090.
DR PDB; 5QYR; X-ray; 1.54 A; A=1836-2090.
DR PDB; 5QYS; X-ray; 1.52 A; A=1836-2090.
DR PDB; 5QYT; X-ray; 1.52 A; A=1836-2090.
DR PDB; 5QYU; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QYV; X-ray; 1.59 A; A=1836-2090.
DR PDB; 5QYW; X-ray; 1.63 A; A=1836-2090.
DR PDB; 5QYX; X-ray; 1.60 A; A=1836-2090.
DR PDB; 5QYY; X-ray; 1.71 A; A=1836-2090.
DR PDB; 5QYZ; X-ray; 1.37 A; A=1836-2090.
DR PDB; 5QZ0; X-ray; 1.57 A; A=1836-2090.
DR PDB; 5QZ1; X-ray; 1.58 A; A=1836-2090.
DR PDB; 5QZ2; X-ray; 1.54 A; A=1836-2090.
DR PDB; 5QZ3; X-ray; 1.53 A; A=1836-2090.
DR PDB; 5QZ4; X-ray; 1.75 A; A=1836-2090.
DR PDB; 5QZ5; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QZ6; X-ray; 1.32 A; A=1836-2090.
DR PDB; 5QZ7; X-ray; 1.48 A; A=1836-2090.
DR PDB; 5QZ8; X-ray; 1.62 A; A=1836-2090.
DR PDB; 5QZ9; X-ray; 1.43 A; A=1836-2090.
DR PDB; 5QZA; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QZB; X-ray; 1.69 A; A=1836-2090.
DR PDB; 5QZC; X-ray; 1.72 A; A=1836-2090.
DR PDB; 5QZD; X-ray; 1.59 A; A=1836-2090.
DR PDB; 5QZE; X-ray; 1.55 A; A=1836-2090.
DR PDB; 5QZF; X-ray; 1.68 A; A=1836-2090.
DR PDB; 5QZG; X-ray; 1.55 A; A=1836-2090.
DR PDB; 5QZH; X-ray; 1.77 A; A=1836-2090.
DR PDB; 5QZI; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QZJ; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5QZK; X-ray; 1.73 A; A=1836-2090.
DR PDB; 5QZL; X-ray; 1.54 A; A=1836-2090.
DR PDB; 5QZM; X-ray; 1.66 A; A=1836-2090.
DR PDB; 5QZN; X-ray; 1.44 A; A=1836-2090.
DR PDB; 5QZO; X-ray; 1.39 A; A=1836-2090.
DR PDB; 5QZP; X-ray; 1.50 A; A=1836-2090.
DR PDB; 5QZQ; X-ray; 2.11 A; A=1836-2090.
DR PDB; 5QZR; X-ray; 1.59 A; A=1836-2090.
DR PDB; 5QZS; X-ray; 1.58 A; A=1836-2090.
DR PDB; 5QZT; X-ray; 1.53 A; A=1836-2090.
DR PDB; 5QZU; X-ray; 1.54 A; A=1836-2090.
DR PDB; 5QZV; X-ray; 2.11 A; A=1836-2090.
DR PDB; 5QZW; X-ray; 1.36 A; A=1836-2090.
DR PDB; 5QZX; X-ray; 1.55 A; A=1836-2090.
DR PDB; 5QZY; X-ray; 1.66 A; A=1836-2090.
DR PDB; 5QZZ; X-ray; 1.59 A; A=1836-2090.
DR PDB; 5R00; X-ray; 1.72 A; A=1836-2090.
DR PDB; 5R01; X-ray; 1.72 A; A=1836-2090.
DR PDB; 5R02; X-ray; 1.66 A; A=1836-2090.
DR PDB; 5R03; X-ray; 1.51 A; A=1836-2090.
DR PDB; 5R04; X-ray; 1.34 A; A=1836-2090.
DR PDB; 5R05; X-ray; 1.57 A; A=1836-2090.
DR PDB; 5R06; X-ray; 1.67 A; A=1836-2090.
DR PDB; 5R07; X-ray; 1.71 A; A=1836-2090.
DR PDB; 5R08; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R09; X-ray; 1.56 A; A=1836-2090.
DR PDB; 5R0A; X-ray; 1.54 A; A=1836-2090.
DR PDB; 5R0B; X-ray; 1.82 A; A=1836-2090.
DR PDB; 5R0C; X-ray; 1.60 A; A=1836-2090.
DR PDB; 5R0D; X-ray; 1.27 A; A=1836-2090.
DR PDB; 5R0E; X-ray; 1.59 A; A=1836-2090.
DR PDB; 5R0F; X-ray; 1.97 A; A=1836-2090.
DR PDB; 5R0G; X-ray; 1.73 A; A=1836-2090.
DR PDB; 5R0H; X-ray; 1.57 A; A=1836-2090.
DR PDB; 5R0I; X-ray; 1.86 A; A=1836-2090.
DR PDB; 5R0J; X-ray; 1.81 A; A=1836-2090.
DR PDB; 5R0K; X-ray; 1.80 A; A=1836-2090.
DR PDB; 5R0L; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R0M; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R0N; X-ray; 1.78 A; A=1836-2090.
DR PDB; 5R0O; X-ray; 1.86 A; A=1836-2090.
DR PDB; 5R0P; X-ray; 1.73 A; A=1836-2090.
DR PDB; 5R0Q; X-ray; 1.91 A; A=1836-2090.
DR PDB; 5R0R; X-ray; 1.73 A; A=1836-2090.
DR PDB; 5R0S; X-ray; 1.81 A; A=1836-2090.
DR PDB; 5R0T; X-ray; 1.96 A; A=1836-2090.
DR PDB; 5R0U; X-ray; 1.86 A; A=1836-2090.
DR PDB; 5R0V; X-ray; 1.81 A; A=1836-2090.
DR PDB; 5R0W; X-ray; 1.86 A; A=1836-2090.
DR PDB; 5R0X; X-ray; 1.84 A; A=1836-2090.
DR PDB; 5R0Y; X-ray; 1.75 A; A=1836-2090.
DR PDB; 5R0Z; X-ray; 1.86 A; A=1836-2090.
DR PDB; 5R10; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R11; X-ray; 1.82 A; A=1836-2090.
DR PDB; 5R12; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R13; X-ray; 1.87 A; A=1836-2090.
DR PDB; 5R14; X-ray; 1.74 A; A=1836-2090.
DR PDB; 5R15; X-ray; 1.79 A; A=1836-2090.
DR PDB; 5R16; X-ray; 1.84 A; A=1836-2090.
DR PDB; 5R17; X-ray; 1.87 A; A=1836-2090.
DR PDB; 5R18; X-ray; 1.79 A; A=1836-2090.
DR PDB; 5R19; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R1A; X-ray; 1.73 A; A=1836-2090.
DR PDB; 5R1B; X-ray; 1.89 A; A=1836-2090.
DR PDB; 5R1C; X-ray; 1.91 A; A=1836-2090.
DR PDB; 5R1D; X-ray; 1.82 A; A=1836-2090.
DR PDB; 5R1E; X-ray; 1.70 A; A=1836-2090.
DR PDB; 5R1F; X-ray; 1.80 A; A=1836-2090.
DR PDB; 5R1G; X-ray; 1.81 A; A=1836-2090.
DR PDB; 5R1H; X-ray; 2.06 A; A=1836-2090.
DR PDB; 5R1I; X-ray; 2.01 A; A=1836-2090.
DR PDB; 5R1J; X-ray; 1.96 A; A=1836-2090.
DR PDB; 5R1K; X-ray; 1.99 A; A=1836-2090.
DR PDB; 5R1L; X-ray; 1.94 A; A=1836-2090.
DR PDB; 5R1M; X-ray; 1.90 A; A=1836-2090.
DR PDB; 5R1N; X-ray; 1.94 A; A=1836-2090.
DR PDB; 5R1O; X-ray; 1.90 A; A=1836-2090.
DR PDB; 5R1P; X-ray; 1.95 A; A=1836-2090.
DR PDB; 5R1Q; X-ray; 1.86 A; A=1836-2090.
DR PDB; 5R1S; X-ray; 2.05 A; A=1836-2090.
DR PDB; 5WSG; EM; 4.00 A; A=1-2413.
DR PDB; 5Y88; EM; 3.70 A; A=1-2413.
DR PDB; 5YLZ; EM; 3.60 A; A=1-2413.
DR PDB; 5ZWM; EM; 3.40 A; A=1-2413.
DR PDB; 5ZWO; EM; 3.90 A; A=1-2413.
DR PDB; 6BK8; EM; 3.30 A; A=1-2413.
DR PDB; 6EXN; EM; 3.70 A; A=1-2413.
DR PDB; 6J6G; EM; 3.20 A; A=1-2413.
DR PDB; 6J6H; EM; 3.60 A; A=1-2413.
DR PDB; 6J6N; EM; 3.86 A; A=1-2413.
DR PDB; 6J6Q; EM; 3.70 A; A=1-2413.
DR PDB; 6TEO; X-ray; 3.10 A; B/D=315-555.
DR PDB; 7B9V; EM; 2.80 A; A=1-2413.
DR PDBsum; 2OG4; -.
DR PDBsum; 3E66; -.
DR PDBsum; 3E9O; -.
DR PDBsum; 3E9P; -.
DR PDBsum; 3JCM; -.
DR PDBsum; 3SBG; -.
DR PDBsum; 3SBT; -.
DR PDBsum; 3ZEF; -.
DR PDBsum; 4BGD; -.
DR PDBsum; 4I43; -.
DR PDBsum; 4ILG; -.
DR PDBsum; 4ILH; -.
DR PDBsum; 4ILJ; -.
DR PDBsum; 5DCA; -.
DR PDBsum; 5GAM; -.
DR PDBsum; 5GAN; -.
DR PDBsum; 5GAO; -.
DR PDBsum; 5GAP; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5M52; -.
DR PDBsum; 5M5P; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5NRL; -.
DR PDBsum; 5QY1; -.
DR PDBsum; 5QY2; -.
DR PDBsum; 5QY3; -.
DR PDBsum; 5QY4; -.
DR PDBsum; 5QY5; -.
DR PDBsum; 5QY6; -.
DR PDBsum; 5QY7; -.
DR PDBsum; 5QY8; -.
DR PDBsum; 5QY9; -.
DR PDBsum; 5QYA; -.
DR PDBsum; 5QYB; -.
DR PDBsum; 5QYC; -.
DR PDBsum; 5QYD; -.
DR PDBsum; 5QYE; -.
DR PDBsum; 5QYF; -.
DR PDBsum; 5QYG; -.
DR PDBsum; 5QYH; -.
DR PDBsum; 5QYI; -.
DR PDBsum; 5QYJ; -.
DR PDBsum; 5QYK; -.
DR PDBsum; 5QYL; -.
DR PDBsum; 5QYM; -.
DR PDBsum; 5QYN; -.
DR PDBsum; 5QYO; -.
DR PDBsum; 5QYP; -.
DR PDBsum; 5QYQ; -.
DR PDBsum; 5QYR; -.
DR PDBsum; 5QYS; -.
DR PDBsum; 5QYT; -.
DR PDBsum; 5QYU; -.
DR PDBsum; 5QYV; -.
DR PDBsum; 5QYW; -.
DR PDBsum; 5QYX; -.
DR PDBsum; 5QYY; -.
DR PDBsum; 5QYZ; -.
DR PDBsum; 5QZ0; -.
DR PDBsum; 5QZ1; -.
DR PDBsum; 5QZ2; -.
DR PDBsum; 5QZ3; -.
DR PDBsum; 5QZ4; -.
DR PDBsum; 5QZ5; -.
DR PDBsum; 5QZ6; -.
DR PDBsum; 5QZ7; -.
DR PDBsum; 5QZ8; -.
DR PDBsum; 5QZ9; -.
DR PDBsum; 5QZA; -.
DR PDBsum; 5QZB; -.
DR PDBsum; 5QZC; -.
DR PDBsum; 5QZD; -.
DR PDBsum; 5QZE; -.
DR PDBsum; 5QZF; -.
DR PDBsum; 5QZG; -.
DR PDBsum; 5QZH; -.
DR PDBsum; 5QZI; -.
DR PDBsum; 5QZJ; -.
DR PDBsum; 5QZK; -.
DR PDBsum; 5QZL; -.
DR PDBsum; 5QZM; -.
DR PDBsum; 5QZN; -.
DR PDBsum; 5QZO; -.
DR PDBsum; 5QZP; -.
DR PDBsum; 5QZQ; -.
DR PDBsum; 5QZR; -.
DR PDBsum; 5QZS; -.
DR PDBsum; 5QZT; -.
DR PDBsum; 5QZU; -.
DR PDBsum; 5QZV; -.
DR PDBsum; 5QZW; -.
DR PDBsum; 5QZX; -.
DR PDBsum; 5QZY; -.
DR PDBsum; 5QZZ; -.
DR PDBsum; 5R00; -.
DR PDBsum; 5R01; -.
DR PDBsum; 5R02; -.
DR PDBsum; 5R03; -.
DR PDBsum; 5R04; -.
DR PDBsum; 5R05; -.
DR PDBsum; 5R06; -.
DR PDBsum; 5R07; -.
DR PDBsum; 5R08; -.
DR PDBsum; 5R09; -.
DR PDBsum; 5R0A; -.
DR PDBsum; 5R0B; -.
DR PDBsum; 5R0C; -.
DR PDBsum; 5R0D; -.
DR PDBsum; 5R0E; -.
DR PDBsum; 5R0F; -.
DR PDBsum; 5R0G; -.
DR PDBsum; 5R0H; -.
DR PDBsum; 5R0I; -.
DR PDBsum; 5R0J; -.
DR PDBsum; 5R0K; -.
DR PDBsum; 5R0L; -.
DR PDBsum; 5R0M; -.
DR PDBsum; 5R0N; -.
DR PDBsum; 5R0O; -.
DR PDBsum; 5R0P; -.
DR PDBsum; 5R0Q; -.
DR PDBsum; 5R0R; -.
DR PDBsum; 5R0S; -.
DR PDBsum; 5R0T; -.
DR PDBsum; 5R0U; -.
DR PDBsum; 5R0V; -.
DR PDBsum; 5R0W; -.
DR PDBsum; 5R0X; -.
DR PDBsum; 5R0Y; -.
DR PDBsum; 5R0Z; -.
DR PDBsum; 5R10; -.
DR PDBsum; 5R11; -.
DR PDBsum; 5R12; -.
DR PDBsum; 5R13; -.
DR PDBsum; 5R14; -.
DR PDBsum; 5R15; -.
DR PDBsum; 5R16; -.
DR PDBsum; 5R17; -.
DR PDBsum; 5R18; -.
DR PDBsum; 5R19; -.
DR PDBsum; 5R1A; -.
DR PDBsum; 5R1B; -.
DR PDBsum; 5R1C; -.
DR PDBsum; 5R1D; -.
DR PDBsum; 5R1E; -.
DR PDBsum; 5R1F; -.
DR PDBsum; 5R1G; -.
DR PDBsum; 5R1H; -.
DR PDBsum; 5R1I; -.
DR PDBsum; 5R1J; -.
DR PDBsum; 5R1K; -.
DR PDBsum; 5R1L; -.
DR PDBsum; 5R1M; -.
DR PDBsum; 5R1N; -.
DR PDBsum; 5R1O; -.
DR PDBsum; 5R1P; -.
DR PDBsum; 5R1Q; -.
DR PDBsum; 5R1S; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 5ZWM; -.
DR PDBsum; 5ZWO; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR PDBsum; 6TEO; -.
DR PDBsum; 7B9V; -.
DR AlphaFoldDB; P33334; -.
DR SMR; P33334; -.
DR BioGRID; 36599; 243.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-29; U5 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-30; U5 small nuclear ribonucleoprotein complex, AAR2 variant.
DR DIP; DIP-2427N; -.
DR IntAct; P33334; 66.
DR MINT; P33334; -.
DR STRING; 4932.YHR165C; -.
DR CarbonylDB; P33334; -.
DR iPTMnet; P33334; -.
DR MaxQB; P33334; -.
DR PaxDb; P33334; -.
DR PRIDE; P33334; -.
DR EnsemblFungi; YHR165C_mRNA; YHR165C; YHR165C.
DR GeneID; 856570; -.
DR KEGG; sce:YHR165C; -.
DR SGD; S000001208; PRP8.
DR VEuPathDB; FungiDB:YHR165C; -.
DR eggNOG; KOG1795; Eukaryota.
DR GeneTree; ENSGT00390000015210; -.
DR HOGENOM; CLU_000380_3_0_1; -.
DR InParanoid; P33334; -.
DR OMA; VCMRREK; -.
DR BioCyc; YEAST:G3O-31199-MON; -.
DR BRENDA; 3.1.13.2; 984.
DR EvolutionaryTrace; P33334; -.
DR PRO; PR:P33334; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P33334; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:SGD.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:SGD.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:SGD.
DR GO; GO:0030623; F:U5 snRNA binding; IDA:SGD.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:SGD.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; IMP:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IC:ComplexPortal.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:SGD.
DR CDD; cd13838; RNase_H_like_Prp8_IV; 1.
DR DisProt; DP02722; -.
DR Gene3D; 1.20.80.40; -; 1.
DR Gene3D; 3.30.420.230; -; 1.
DR Gene3D; 3.30.43.40; -; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR012591; PRO8NT.
DR InterPro; IPR012592; PROCN.
DR InterPro; IPR012984; PROCT.
DR InterPro; IPR027652; PRP8.
DR InterPro; IPR021983; PRP8_domainIV.
DR InterPro; IPR043173; Prp8_domainIV_fingers.
DR InterPro; IPR043172; Prp8_domainIV_palm.
DR InterPro; IPR019581; Prp8_U5-snRNA-bd.
DR InterPro; IPR042516; Prp8_U5-snRNA-bd_sf.
DR InterPro; IPR019580; Prp8_U6-snRNA-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR019582; RRM_spliceosomal_PrP8.
DR PANTHER; PTHR11140; PTHR11140; 1.
DR Pfam; PF08082; PRO8NT; 1.
DR Pfam; PF08083; PROCN; 1.
DR Pfam; PF08084; PROCT; 1.
DR Pfam; PF12134; PRP8_domainIV; 1.
DR Pfam; PF10598; RRM_4; 1.
DR Pfam; PF10597; U5_2-snRNA_bdg; 1.
DR Pfam; PF10596; U6-snRNA_bdg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..2413
FT /note="Pre-mRNA-splicing factor 8"
FT /id="PRO_0000097042"
FT DOMAIN 2182..2311
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..543
FT /note="SNU114/CWC21 interacting domain (SCwid)"
FT REGION 885..1375
FT /note="Reverse transcriptase homology domain"
FT REGION 1376..1649
FT /note="Linker"
FT REGION 1585..1598
FT /note="Important for branch point selection"
FT REGION 1653..1824
FT /note="Restriction endonuclease homology domain"
FT REGION 1839..2092
FT /note="RNase H homology domain"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1658
FT /note="H->S: No effect on viability."
FT /evidence="ECO:0000269|PubMed:23354046"
FT MUTAGEN 1684
FT /note="E->Q: No effect on viability."
FT /evidence="ECO:0000269|PubMed:23354046"
FT MUTAGEN 1687
FT /note="H->S: No effect on viability."
FT /evidence="ECO:0000269|PubMed:23354046"
FT MUTAGEN 1700
FT /note="D->N: No effect on viability."
FT /evidence="ECO:0000269|PubMed:23354046"
FT MUTAGEN 1735
FT /note="D->N: No effect on viability."
FT /evidence="ECO:0000269|PubMed:23354046"
FT MUTAGEN 1853
FT /note="D->A: Alters protein folding. Severely impaired
FT growth. Strongly reduced growth at 35 degrees Celsius; when
FT associated with A-1854."
FT /evidence="ECO:0000269|PubMed:18779563,
FT ECO:0000269|PubMed:18836455, ECO:0000269|PubMed:18843295"
FT MUTAGEN 1853
FT /note="D->N: Reduced growth at 30 degrees Celsius. Strongly
FT reduced growth at 16 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:18779563,
FT ECO:0000269|PubMed:18836455, ECO:0000269|PubMed:18843295"
FT MUTAGEN 1854
FT /note="D->A: Reduced growth at 30 degrees Celsius. Strongly
FT reduced growth at 16 degrees Celsius. Strongly reduced
FT growth at 35 degrees Celsius; when associated with A-1853."
FT /evidence="ECO:0000269|PubMed:18836455,
FT ECO:0000269|PubMed:18843295"
FT MUTAGEN 1854
FT /note="D->N: Reduced growth at 30 degrees Celsius. Strongly
FT reduced growth at 16 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:18836455,
FT ECO:0000269|PubMed:18843295"
FT MUTAGEN 1855
FT /note="T->A: Reduced growth at 30 degrees Celsius. Strongly
FT reduced growth at 16 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:18843295"
FT MUTAGEN 1936
FT /note="T->A: Reduced growth at 30 degrees Celsius. Strongly
FT reduced growth at 16 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:18843295"
FT MUTAGEN 1937
FT /note="R->K: Severely impaired growth. Reduced growth at 30
FT degrees Celsius. Strongly reduced growth at 16 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:18843295"
FT CONFLICT 388..420
FT /note="PHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTP -> LIYIIPGPVQCAYHG
FT IIIQCRVLSRTMRSTTRL (in Ref. 2; AAA67044)"
FT /evidence="ECO:0000305"
FT CONFLICT 1132
FT /note="T -> S (in Ref. 2; AAA67044)"
FT /evidence="ECO:0000305"
FT CONFLICT 1575
FT /note="W -> C (in Ref. 2; AAA67044)"
FT /evidence="ECO:0000305"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 163..167
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 210..230
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 274..281
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 388..392
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 473..480
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 496..507
FT /evidence="ECO:0007829|PDB:6TEO"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:6TEO"
FT HELIX 519..532
FT /evidence="ECO:0007829|PDB:6TEO"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 547..552
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 564..585
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 607..612
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 617..640
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 646..657
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 660..663
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 674..691
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 692..694
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 705..735
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 750..769
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 778..794
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 806..836
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 842..870
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 885..892
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 908..924
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 931..945
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 947..960
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 975..983
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 986..1005
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1017..1019
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 1021..1033
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1036..1039
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1042..1044
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 1046..1053
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1056..1060
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1063..1071
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1076..1085
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1087..1092
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1095..1098
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1110..1135
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1138..1140
FT /evidence="ECO:0007829|PDB:3ZEF"
FT HELIX 1150..1154
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1156..1164
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1167..1174
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1176..1189
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1197..1200
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1205..1207
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 1209..1211
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1217..1231
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1236..1238
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1243..1245
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1246..1252
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1258..1262
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1265..1271
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1272..1274
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1275..1277
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 1283..1289
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1291..1293
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1295..1304
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1306..1320
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1328..1346
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1348..1351
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1354..1375
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1380..1382
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1385..1389
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1392..1394
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1409..1412
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1414..1417
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1422..1425
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1427..1429
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1434..1436
FT /evidence="ECO:0007829|PDB:3ZEF"
FT HELIX 1440..1443
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1447..1470
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1477..1479
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1480..1482
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1487..1490
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1491..1495
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1499..1502
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1508..1514
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1515..1517
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1530..1533
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1540..1549
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1552..1558
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1559..1561
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 1563..1565
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1568..1575
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 1581..1585
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1592..1595
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1598..1600
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1603..1614
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1617..1619
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1624..1626
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 1628..1630
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 1633..1636
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1641..1648
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1649..1652
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1653..1670
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1671..1677
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1678..1683
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1690..1692
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1700..1711
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1726..1739
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1743..1745
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1748..1759
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1763..1766
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1768..1778
FT /evidence="ECO:0007829|PDB:4I43"
FT TURN 1779..1782
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1783..1788
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1794..1808
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 1810..1822
FT /evidence="ECO:0007829|PDB:4I43"
FT STRAND 1825..1827
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 1837..1844
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1845..1847
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1849..1853
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1857..1864
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1866..1868
FT /evidence="ECO:0007829|PDB:4ILG"
FT STRAND 1870..1875
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1877..1882
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 1884..1886
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1888..1894
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1896..1899
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1905..1923
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1926..1928
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1931..1937
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1938..1940
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1941..1947
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 1948..1950
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1954..1957
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1959..1961
FT /evidence="ECO:0007829|PDB:5QZ6"
FT HELIX 1965..1970
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1972..1980
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 1985..1990
FT /evidence="ECO:0007829|PDB:5R0D"
FT TURN 1991..1994
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 1995..1997
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 2001..2017
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 2019..2027
FT /evidence="ECO:0007829|PDB:5R0D"
FT STRAND 2030..2032
FT /evidence="ECO:0007829|PDB:3E9P"
FT STRAND 2039..2041
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 2045..2067
FT /evidence="ECO:0007829|PDB:5R0D"
FT HELIX 2071..2073
FT /evidence="ECO:0007829|PDB:5QY2"
FT HELIX 2076..2085
FT /evidence="ECO:0007829|PDB:5QY2"
FT STRAND 2088..2090
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 2091..2105
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 2149..2159
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2160..2167
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2168..2171
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2178..2180
FT /evidence="ECO:0007829|PDB:5DCA"
FT STRAND 2182..2186
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2187..2195
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2199..2201
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2204..2211
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2218..2225
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2229..2231
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2236..2238
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2245..2247
FT /evidence="ECO:0007829|PDB:3ZEF"
FT STRAND 2254..2264
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2271..2281
FT /evidence="ECO:0007829|PDB:2OG4"
FT TURN 2282..2284
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2289..2296
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2299..2307
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2309..2316
FT /evidence="ECO:0007829|PDB:2OG4"
FT TURN 2317..2320
FT /evidence="ECO:0007829|PDB:3SBG"
FT TURN 2323..2325
FT /evidence="ECO:0007829|PDB:4BGD"
FT HELIX 2331..2333
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2334..2345
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2348..2352
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2360..2362
FT /evidence="ECO:0007829|PDB:4I43"
FT HELIX 2363..2365
FT /evidence="ECO:0007829|PDB:2OG4"
FT STRAND 2374..2376
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2385..2387
FT /evidence="ECO:0007829|PDB:2OG4"
FT HELIX 2389..2396
FT /evidence="ECO:0007829|PDB:5DCA"
FT TURN 2406..2408
FT /evidence="ECO:0007829|PDB:5M52"
SQ SEQUENCE 2413 AA; 279504 MW; 8F4F6F89D34D3508 CRC64;
MSGLPPPPPG FEEDSDLALP PPPPPPPGYE IEELDNPMVP SSVNEDTFLP PPPPPPSNFE
INAEEIVDFT LPPPPPPPGL DELETKAEKK VELHGKRKLD IGKDTFVTRK SRKRAKKMTK
KAKRSNLYTP KAEMPPEHLR KIINTHSDMA SKMYNTDKKA FLGALKYLPH AILKLLENMP
HPWEQAKEVK VLYHTSGAIT FVNETPRVIE PVYTAQWSAT WIAMRREKRD RTHFKRMRFP
PFDDDEPPLS YEQHIENIEP LDPINLPLDS QDDEYVKDWL YDSRPLEEDS KKVNGTSYKK
WSFDLPEMSN LYRLSTPLRD EVTDKNYYYL FDKKSFFNGK ALNNAIPGGP KFEPLYPREE
EEDYNEFNSI DRVIFRVPIR SEYKVAFPHL YNSRPRSVRI PWYNNPVSCI IQNDEEYDTP
ALFFDPSLNP IPHFIDNNSS LNVSNTKENG DFTLPEDFAP LLAEEEELIL PNTKDAMSLY
HSPFPFNRTK GKMVRAQDVA LAKKWFLQHP DEEYPVKVKV SYQKLLKNYV LNELHPTLPT
NHNKTKLLKS LKNTKYFQQT TIDWVEAGLQ LCRQGHNMLN LLIHRKGLTY LHLDYNFNLK
PTKTLTTKER KKSRLGNSFH LMRELLKMMK LIVDTHVQFR LGNVDAFQLA DGIHYILNHI
GQLTGIYRYK YKVMHQIRAC KDLKHIIYYK FNKNLGKGPG CGFWQPAWRV WLNFLRGTIP
LLERYIGNLI TRQFEGRSNE IVKTTTKQRL DAYYDLELRN SVMDDILEMM PESIRQKKAR
TILQHLSEAW RCWKANIPWD VPGMPAPIKK IIERYIKSKA DAWVSAAHYN RERIKRGAHV
EKTMVKKNLG RLTRLWIKNE QERQRQIQKN GPEITPEEAT TIFSVMVEWL ESRSFSPIPF
PPLTYKNDTK ILVLALEDLK DVYASKVRLN ASEREELALI EEAYDNPHDT LNRIKKYLLT
QRVFKPVDIT MMENYQNISP VYSVDPLEKI TDAYLDQYLW YEADQRKLFP NWIKPSDSEI
PPLLVYKWTQ GINNLSEIWD VSRGQSAVLL ETTLGEMAEK IDFTLLNRLL RLIVDPNIAD
YITAKNNVVI NFKDMSHVNK YGLIRGLKFA SFIFQYYGLV IDLLLLGQER ATDLAGPANN
PNEFMQFKSK EVEKAHPIRL YTRYLDRIYM LFHFEEDEGE ELTDEYLAEN PDPNFENSIG
YNNRKCWPKD SRMRLIRQDV NLGRAVFWEI QSRVPTSLTS IKWENAFVSV YSKNNPNLLF
SMCGFEVRIL PRQRMEEVVS NDEGVWDLVD ERTKQRTAKA YLKVSEEEIK KFDSRIRGIL
MASGSTTFTK VAAKWNTSLI SLFTYFREAI VATEPLLDIL VKGETRIQNR VKLGLNSKMP
TRFPPAVFYT PKELGGLGMI SASHILIPAS DLSWSKQTDT GITHFRAGMT HEDEKLIPTI
FRYITTWENE FLDSQRVWAE YATKRQEAIQ QNRRLAFEEL EGSWDRGIPR ISTLFQRDRH
TLAYDRGHRI RREFKQYSLE RNSPFWWTNS HHDGKLWNLN AYRTDVIQAL GGIETILEHT
LFKGTGFNSW EGLFWEKASG FEDSMQFKKL THAQRTGLSQ IPNRRFTLWW SPTINRANVY
VGFLVQLDLT GIFLHGKIPT LKISLIQIFR AHLWQKIHES IVFDICQILD GELDVLQIES
VTKETVHPRK SYKMNSSAAD ITMESVHEWE VSKPSLLHET NDSFKGLITN KMWFDVQLRY
GDYDSHDISR YVRAKFLDYT TDNVSMYPSP TGVMIGIDLA YNMYDAYGNW FNGLKPLIQN
SMRTIMKANP ALYVLRERIR KGLQIYQSSV QEPFLNSSNY AELFNNDIKL FVDDTNVYRV
TVHKTFEGNV ATKAINGCIF TLNPKTGHLF LKIIHTSVWA GQKRLSQLAK WKTAEEVSAL
VRSLPKEEQP KQIIVTRKAM LDPLEVHMLD FPNIAIRPTE LRLPFSAAMS IDKLSDVVMK
ATEPQMVLFN IYDDWLDRIS SYTAFSRLTL LLRALKTNEE SAKMILLSDP TITIKSYHLW
PSFTDEQWIT IESQMRDLIL TEYGRKYNVN ISALTQTEIK DIILGQNIKA PSVKRQKMAE
LEAARSEKQN DEEAAGASTV MKTKTINAQG EEIVVVASAD YESQTFSSKN EWRKSAIANT
LLYLRLKNIY VSADDFVEEQ NVYVLPKNLL KKFIEISDVK IQVAAFIYGM SAKDHPKVKE
IKTVVLVPQL GHVGSVQISN IPDIGDLPDT EGLELLGWIH TQTEELKFMA ASEVATHSKL
FADKKRDCID ISIFSTPGSV SLSAYNLTDE GYQWGEENKD IMNVLSEGFE PTFSTHAQLL
LSDRITGNFI IPSGNVWNYT FMGTAFNQEG DYNFKYGIPL EFYNEMHRPV HFLQFSELAG
DEELEAEQID VFS
