ID PSA6_YEAST Reviewed; 234 AA.
AC P40302; D6W0E1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 230.
DE RecName: Full=Proteasome subunit alpha type-6;
DE AltName: Full=Macropain subunit PRE5;
DE AltName: Full=Multicatalytic endopeptidase complex subunit PRE5;
DE AltName: Full=Proteasome component PRE5;
DE AltName: Full=Proteinase YSCE subunit PRE5;
GN Name=PRE5; OrderedLocusNames=YMR314W; ORFNames=YM9924.06;
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], AND PROTEIN SEQUENCE OF 141-149 AND
RP 220-228.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7918444; DOI=10.1021/bi00206a028;
RA Heinemeyer W., Troendle N., Albrecht G., Wolf D.H.;
RT "PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits
RT from yeast? Indication for a set of 14 different subunits in the eukaryotic
RT proteasome core.";
RL Biochemistry 33:12229-12237(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
RX PubMed=9087403; DOI=10.1038/386463a0;
RA Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D.,
RA Huber R.;
RT "Structure of 20S proteasome from yeast at 2.4-A resolution.";
RL Nature 386:463-471(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME
RP AND A 11S REGULATORY COMPLEX.
RX PubMed=11081519; DOI=10.1038/35040607;
RA Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C.,
RA Hill C.P.;
RT "Structural basis for the activation of 20S proteasomes by 11S
RT regulators.";
RL Nature 408:115-120(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
RX PubMed=11062564; DOI=10.1038/80992;
RA Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R.,
RA Glickman M.H., Finley D.;
RT "A gated channel into the proteasome core particle.";
RL Nat. Struct. Biol. 7:1062-1067(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME
RP AND A TMC-95-BASED INHIBITOR.
RX PubMed=16793518; DOI=10.1016/j.chembiol.2006.04.005;
RA Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.;
RT "TMC-95-based inhibitor design provides evidence for the catalytic
RT versatility of the proteasome.";
RL Chem. Biol. 13:607-614(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME
RP AND SALINOSPORAMIDE.
RX PubMed=16608349; DOI=10.1021/ja058320b;
RA Groll M., Huber R., Potts B.C.M.;
RT "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in
RT complex with the 20S proteasome reveal important consequences of beta-
RT lactone ring opening and a mechanism for irreversible binding.";
RL J. Am. Chem. Soc. 128:5136-5141(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME
RP AND BORTEZOMIB.
RX PubMed=16531229; DOI=10.1016/j.str.2005.11.019;
RA Groll M., Berkers C.R., Ploegh H.L., Ovaa H.;
RT "Crystal structure of the boronic acid-based proteasome inhibitor
RT bortezomib in complex with the yeast 20S proteasome.";
RL Structure 14:451-456(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH THE PROTEASOME.
RX PubMed=20227375; DOI=10.1016/j.molcel.2010.02.002;
RA Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.;
RT "Structure of a Blm10 complex reveals common mechanisms for proteasome
RT binding and gate opening.";
RL Mol. Cell 37:728-735(2010).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
RX PubMed=22927375; DOI=10.1073/pnas.1213333109;
RA Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E.,
RA Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.;
RT "Near-atomic resolution structural model of the yeast 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012).
CC -!- FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the
CC cytoplasm and in the nucleus. It is essential for the regulated
CC turnover of proteins and for the removal of misfolded proteins. The
CC proteasome is a multicatalytic proteinase complex that is characterized
CC by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu
CC adjacent to the leaving group at neutral or slightly basic pH. It has
CC an ATP-dependent proteolytic activity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000269|PubMed:20227375}.
CC -!- INTERACTION:
CC P40302; Q12245: POC4; NbExp=2; IntAct=EBI-13955, EBI-2343020;
CC P40302; P30656: PRE2; NbExp=2; IntAct=EBI-13955, EBI-14001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 7210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; L34347; AAA53544.1; -; Genomic_DNA.
DR EMBL; Z54141; CAA90832.1; -; Genomic_DNA.
DR EMBL; AY557978; AAS56304.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10215.1; -; Genomic_DNA.
DR PIR; A55904; A55904.
DR RefSeq; NP_014045.1; NM_001182825.1.
DR PDB; 1FNT; X-ray; 3.20 A; F/T=1-234.
DR PDB; 1G0U; X-ray; 2.40 A; E/S=1-234.
DR PDB; 1G65; X-ray; 2.25 A; E/S=2-234.
DR PDB; 1JD2; X-ray; 3.00 A; E/Z=2-234.
DR PDB; 1RYP; X-ray; 1.90 A; F/T=2-234.
DR PDB; 1Z7Q; X-ray; 3.22 A; F/T=1-234.
DR PDB; 2F16; X-ray; 2.80 A; E/S=2-234.
DR PDB; 2FAK; X-ray; 2.80 A; E/S=2-234.
DR PDB; 2GPL; X-ray; 2.81 A; E/S=2-234.
DR PDB; 2ZCY; X-ray; 2.90 A; E/S=1-234.
DR PDB; 3BDM; X-ray; 2.70 A; E/S=1-234.
DR PDB; 3D29; X-ray; 2.60 A; E/S=2-234.
DR PDB; 3DY3; X-ray; 2.81 A; E/S=2-234.
DR PDB; 3DY4; X-ray; 2.80 A; E/S=2-234.
DR PDB; 3E47; X-ray; 3.00 A; E/S=2-234.
DR PDB; 3GPJ; X-ray; 2.70 A; E/S=2-234.
DR PDB; 3GPT; X-ray; 2.41 A; E/S=2-234.
DR PDB; 3GPW; X-ray; 2.50 A; E/S=2-234.
DR PDB; 3HYE; X-ray; 2.50 A; E/S=2-234.
DR PDB; 3JCO; EM; 4.80 A; F/f=1-234.
DR PDB; 3JCP; EM; 4.60 A; F/f=1-234.
DR PDB; 3MG0; X-ray; 2.68 A; E/S=2-234.
DR PDB; 3MG4; X-ray; 3.11 A; E/S=2-234.
DR PDB; 3MG6; X-ray; 2.60 A; E/S=1-234.
DR PDB; 3MG7; X-ray; 2.78 A; E/S=1-234.
DR PDB; 3MG8; X-ray; 2.59 A; E/S=1-234.
DR PDB; 3NZJ; X-ray; 2.40 A; E/S=1-234.
DR PDB; 3NZW; X-ray; 2.50 A; E/S=1-234.
DR PDB; 3NZX; X-ray; 2.70 A; E/S=1-234.
DR PDB; 3OEU; X-ray; 2.60 A; E/S=2-234.
DR PDB; 3OEV; X-ray; 2.85 A; E/S=2-234.
DR PDB; 3OKJ; X-ray; 2.70 A; E/S=2-234.
DR PDB; 3SDI; X-ray; 2.65 A; E/S=2-234.
DR PDB; 3SDK; X-ray; 2.70 A; E/S=2-234.
DR PDB; 3SHJ; X-ray; 2.80 A; E/S=2-234.
DR PDB; 3TDD; X-ray; 2.70 A; E/S=2-234.
DR PDB; 3UN4; X-ray; 3.40 A; E/S=1-234.
DR PDB; 3UN8; X-ray; 2.70 A; E/S=1-234.
DR PDB; 3WXR; X-ray; 3.15 A; F/T=1-234.
DR PDB; 4CR2; EM; 7.70 A; F=1-234.
DR PDB; 4CR3; EM; 9.30 A; F=1-234.
DR PDB; 4CR4; EM; 8.80 A; F=1-234.
DR PDB; 4EU2; X-ray; 2.51 A; F/T=2-234.
DR PDB; 4FZC; X-ray; 2.80 A; E/S=2-234.
DR PDB; 4FZG; X-ray; 3.00 A; E/S=2-234.
DR PDB; 4G4S; X-ray; 2.49 A; F=1-234.
DR PDB; 4GK7; X-ray; 2.80 A; E/S=2-234.
DR PDB; 4HNP; X-ray; 2.80 A; E/S=2-234.
DR PDB; 4HRC; X-ray; 2.80 A; E/S=2-234.
DR PDB; 4HRD; X-ray; 2.80 A; E/S=2-234.
DR PDB; 4INR; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4INT; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4INU; X-ray; 3.10 A; E/S=1-234.
DR PDB; 4J70; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4JSQ; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4JSU; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4JT0; X-ray; 3.10 A; E/S=1-234.
DR PDB; 4LQI; X-ray; 2.70 A; E/S=2-234.
DR PDB; 4LTC; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4NNN; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4NNW; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4NO1; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4NO6; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4NO8; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4NO9; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4Q1S; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QBY; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QLQ; X-ray; 2.40 A; E/S=1-234.
DR PDB; 4QLS; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QLT; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QLU; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QLV; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QUX; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QUY; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QV0; X-ray; 3.10 A; E/S=1-234.
DR PDB; 4QV1; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4QV3; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QV4; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4QV5; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4QV6; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QV7; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QV8; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QV9; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QVL; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QVM; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QVN; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QVP; X-ray; 2.30 A; E/S=1-234.
DR PDB; 4QVQ; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QVV; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QVW; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QVY; X-ray; 2.51 A; E/S=1-234.
DR PDB; 4QW0; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QW1; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QW3; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QW4; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QW5; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QW6; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QW7; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4QWF; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QWG; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QWI; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QWJ; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QWK; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QWL; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QWR; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QWS; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QWU; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QWX; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QXJ; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QZ0; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QZ1; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QZ2; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4QZ3; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QZ4; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QZ5; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QZ6; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4QZ7; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4QZW; X-ray; 3.00 A; E/S=1-234.
DR PDB; 4QZX; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4QZZ; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4R00; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4R02; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4R17; X-ray; 2.10 A; E/S=1-234.
DR PDB; 4R18; X-ray; 2.40 A; E/S=1-234.
DR PDB; 4RUR; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4V7O; X-ray; 3.00 A; AK/AW/BF/BT=1-234.
DR PDB; 4X6Z; X-ray; 2.70 A; F/T=1-234.
DR PDB; 4Y69; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4Y6A; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y6V; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y6Z; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y70; X-ray; 2.40 A; E/S=1-234.
DR PDB; 4Y74; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y75; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y77; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4Y78; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y7W; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4Y7X; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y7Y; X-ray; 2.40 A; E/S=1-234.
DR PDB; 4Y80; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4Y81; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y82; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y84; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y8G; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y8H; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4Y8I; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y8J; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y8K; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y8L; X-ray; 2.40 A; E/S=1-234.
DR PDB; 4Y8M; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y8N; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y8O; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y8P; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y8Q; X-ray; 2.60 A; E/S=1-234.
DR PDB; 4Y8R; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y8S; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y8T; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Y8U; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4Y9Y; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4Y9Z; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4YA0; X-ray; 2.80 A; E/S=1-234.
DR PDB; 4YA1; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4YA2; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4YA3; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4YA4; X-ray; 2.90 A; E/S=1-234.
DR PDB; 4YA5; X-ray; 2.50 A; E/S=1-234.
DR PDB; 4YA7; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4YA9; X-ray; 2.70 A; E/S=1-234.
DR PDB; 4Z1L; X-ray; 3.00 A; E/S=1-234.
DR PDB; 5A5B; EM; 9.50 A; F=1-234.
DR PDB; 5AHJ; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5BOU; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5BXL; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5BXN; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5CGF; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5CGG; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5CGH; X-ray; 2.50 A; E/S=1-234.
DR PDB; 5CGI; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5CZ4; X-ray; 2.30 A; E/S=1-234.
DR PDB; 5CZ5; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5CZ6; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5CZ7; X-ray; 2.50 A; E/S=1-234.
DR PDB; 5CZ8; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5CZ9; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5CZA; X-ray; 2.50 A; E/S=1-234.
DR PDB; 5D0S; X-ray; 2.50 A; E/S=1-234.
DR PDB; 5D0T; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5D0V; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5D0W; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5D0X; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5D0Z; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5DKI; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5DKJ; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5FG7; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5FG9; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5FGA; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5FGD; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5FGE; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5FGF; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5FGG; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5FGH; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5FGI; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5FHS; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5JHR; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5JHS; X-ray; 3.00 A; E/S=1-234.
DR PDB; 5L52; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L54; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L55; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5A; X-ray; 2.40 A; E/S=1-234.
DR PDB; 5L5B; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L5D; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L5E; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5F; X-ray; 2.50 A; E/S=1-234.
DR PDB; 5L5H; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5L5I; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5J; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5O; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5L5P; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L5Q; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L5R; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5S; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5L5T; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5U; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5L5V; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L5W; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L5X; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L5Y; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L5Z; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L60; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L61; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L62; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L63; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L64; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L65; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5L66; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L67; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5L68; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L69; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5L6A; X-ray; 2.80 A; E/S=1-234.
DR PDB; 5L6B; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5L6C; X-ray; 2.60 A; E/S=1-234.
DR PDB; 5LAI; X-ray; 2.50 A; E/S=1-234.
DR PDB; 5LAJ; X-ray; 2.90 A; E/S=1-234.
DR PDB; 5LTT; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5M2B; X-ray; 2.70 A; E/S=1-234.
DR PDB; 5MP9; EM; 4.10 A; F/f=1-234.
DR PDB; 5MPA; EM; 4.50 A; F/f=1-234.
DR PDB; 5MPB; EM; 7.80 A; F/f=1-234.
DR PDB; 5MPC; EM; 7.70 A; F/f=1-234.
DR PDB; 5NIF; X-ray; 3.00 A; F/T=1-234.
DR PDB; 5WVI; EM; 6.30 A; F/l=1-234.
DR PDB; 5WVK; EM; 4.20 A; F/l=1-234.
DR PDB; 6EF0; EM; 4.43 A; F=1-234.
DR PDB; 6EF1; EM; 4.73 A; F=2-234.
DR PDB; 6EF2; EM; 4.27 A; F=3-234.
DR PDB; 6EF3; EM; 4.17 A; F=1-234.
DR PDB; 6FVT; EM; 4.10 A; F/f=4-234.
DR PDB; 6FVU; EM; 4.50 A; F/f=4-234.
DR PDB; 6FVV; EM; 5.40 A; F/f=4-234.
DR PDB; 6FVW; EM; 4.50 A; F/f=3-234.
DR PDB; 6FVX; EM; 4.90 A; F/f=3-234.
DR PDB; 6FVY; EM; 6.10 A; F/f=3-234.
DR PDB; 6G7F; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6G8M; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6G8N; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6GOP; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6H39; X-ray; 2.50 A; E/S=1-234.
DR PDB; 6HTB; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HTC; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HTD; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HTP; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HTR; X-ray; 2.60 A; E/S=1-234.
DR PDB; 6HUB; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6HUC; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HUQ; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HUU; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HUV; X-ray; 3.10 A; E/S=1-234.
DR PDB; 6HV3; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HV4; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HV5; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HV7; X-ray; 3.40 A; E/S=1-234.
DR PDB; 6HVA; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6HVR; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HVS; X-ray; 3.10 A; E/S=1-234.
DR PDB; 6HVT; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6HVU; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6HVV; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HVW; X-ray; 3.00 A; E/S=1-234.
DR PDB; 6HVX; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HVY; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HW0; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HW3; X-ray; 2.60 A; E/S=1-234.
DR PDB; 6HW4; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6HW5; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6HW6; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HW7; X-ray; 2.70 A; E/S=1-234.
DR PDB; 6HW8; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HW9; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HWA; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HWB; X-ray; 2.60 A; E/S=1-234.
DR PDB; 6HWC; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HWD; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6HWE; X-ray; 2.30 A; E/S=1-234.
DR PDB; 6HWF; X-ray; 2.50 A; E/S=1-234.
DR PDB; 6J2C; EM; 7.00 A; F/l=1-234.
DR PDB; 6J2N; EM; 7.50 A; F/l=1-234.
DR PDB; 6J2Q; EM; 3.80 A; F/l=1-234.
DR PDB; 6J2X; EM; 3.80 A; F/l=1-234.
DR PDB; 6J30; EM; 4.50 A; F/l=1-234.
DR PDB; 6ZOU; X-ray; 2.90 A; E/S=1-234.
DR PDB; 6ZP6; X-ray; 2.80 A; E/S=1-234.
DR PDB; 6ZP8; X-ray; 3.00 A; E/S=1-234.
DR PDB; 7LS5; EM; 2.74 A; F/T=1-234.
DR PDB; 7LS6; EM; 3.17 A; F=1-234.
DR PDB; 7LSX; EM; 3.61 A; F=1-234.
DR PDB; 7O2L; X-ray; 3.00 A; E/S=1-234.
DR PDB; 7QO3; EM; 6.10 A; F/f=1-234.
DR PDB; 7QO5; EM; 6.00 A; F/f=1-234.
DR PDB; 7TEJ; EM; 2.74 A; F/T=1-234.
DR PDB; 7TEO; EM; 2.97 A; F/T=1-234.
DR PDB; 8OLR; X-ray; 2.80 A; E/S=1-234.
DR PDB; 8T08; EM; 3.00 A; F/W=1-234.
DR PDB; 8T0M; EM; 2.40 A; F/T=1-234.
DR PDBsum; 1FNT; -.
DR PDBsum; 1G0U; -.
DR PDBsum; 1G65; -.
DR PDBsum; 1JD2; -.
DR PDBsum; 1RYP; -.
DR PDBsum; 1Z7Q; -.
DR PDBsum; 2F16; -.
DR PDBsum; 2FAK; -.
DR PDBsum; 2GPL; -.
DR PDBsum; 2ZCY; -.
DR PDBsum; 3BDM; -.
DR PDBsum; 3D29; -.
DR PDBsum; 3DY3; -.
DR PDBsum; 3DY4; -.
DR PDBsum; 3E47; -.
DR PDBsum; 3GPJ; -.
DR PDBsum; 3GPT; -.
DR PDBsum; 3GPW; -.
DR PDBsum; 3HYE; -.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 3MG0; -.
DR PDBsum; 3MG4; -.
DR PDBsum; 3MG6; -.
DR PDBsum; 3MG7; -.
DR PDBsum; 3MG8; -.
DR PDBsum; 3NZJ; -.
DR PDBsum; 3NZW; -.
DR PDBsum; 3NZX; -.
DR PDBsum; 3OEU; -.
DR PDBsum; 3OEV; -.
DR PDBsum; 3OKJ; -.
DR PDBsum; 3SDI; -.
DR PDBsum; 3SDK; -.
DR PDBsum; 3SHJ; -.
DR PDBsum; 3TDD; -.
DR PDBsum; 3UN4; -.
DR PDBsum; 3UN8; -.
DR PDBsum; 3WXR; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 4EU2; -.
DR PDBsum; 4FZC; -.
DR PDBsum; 4FZG; -.
DR PDBsum; 4G4S; -.
DR PDBsum; 4GK7; -.
DR PDBsum; 4HNP; -.
DR PDBsum; 4HRC; -.
DR PDBsum; 4HRD; -.
DR PDBsum; 4INR; -.
DR PDBsum; 4INT; -.
DR PDBsum; 4INU; -.
DR PDBsum; 4J70; -.
DR PDBsum; 4JSQ; -.
DR PDBsum; 4JSU; -.
DR PDBsum; 4JT0; -.
DR PDBsum; 4LQI; -.
DR PDBsum; 4LTC; -.
DR PDBsum; 4NNN; -.
DR PDBsum; 4NNW; -.
DR PDBsum; 4NO1; -.
DR PDBsum; 4NO6; -.
DR PDBsum; 4NO8; -.
DR PDBsum; 4NO9; -.
DR PDBsum; 4Q1S; -.
DR PDBsum; 4QBY; -.
DR PDBsum; 4QLQ; -.
DR PDBsum; 4QLS; -.
DR PDBsum; 4QLT; -.
DR PDBsum; 4QLU; -.
DR PDBsum; 4QLV; -.
DR PDBsum; 4QUX; -.
DR PDBsum; 4QUY; -.
DR PDBsum; 4QV0; -.
DR PDBsum; 4QV1; -.
DR PDBsum; 4QV3; -.
DR PDBsum; 4QV4; -.
DR PDBsum; 4QV5; -.
DR PDBsum; 4QV6; -.
DR PDBsum; 4QV7; -.
DR PDBsum; 4QV8; -.
DR PDBsum; 4QV9; -.
DR PDBsum; 4QVL; -.
DR PDBsum; 4QVM; -.
DR PDBsum; 4QVN; -.
DR PDBsum; 4QVP; -.
DR PDBsum; 4QVQ; -.
DR PDBsum; 4QVV; -.
DR PDBsum; 4QVW; -.
DR PDBsum; 4QVY; -.
DR PDBsum; 4QW0; -.
DR PDBsum; 4QW1; -.
DR PDBsum; 4QW3; -.
DR PDBsum; 4QW4; -.
DR PDBsum; 4QW5; -.
DR PDBsum; 4QW6; -.
DR PDBsum; 4QW7; -.
DR PDBsum; 4QWF; -.
DR PDBsum; 4QWG; -.
DR PDBsum; 4QWI; -.
DR PDBsum; 4QWJ; -.
DR PDBsum; 4QWK; -.
DR PDBsum; 4QWL; -.
DR PDBsum; 4QWR; -.
DR PDBsum; 4QWS; -.
DR PDBsum; 4QWU; -.
DR PDBsum; 4QWX; -.
DR PDBsum; 4QXJ; -.
DR PDBsum; 4QZ0; -.
DR PDBsum; 4QZ1; -.
DR PDBsum; 4QZ2; -.
DR PDBsum; 4QZ3; -.
DR PDBsum; 4QZ4; -.
DR PDBsum; 4QZ5; -.
DR PDBsum; 4QZ6; -.
DR PDBsum; 4QZ7; -.
DR PDBsum; 4QZW; -.
DR PDBsum; 4QZX; -.
DR PDBsum; 4QZZ; -.
DR PDBsum; 4R00; -.
DR PDBsum; 4R02; -.
DR PDBsum; 4R17; -.
DR PDBsum; 4R18; -.
DR PDBsum; 4RUR; -.
DR PDBsum; 4V7O; -.
DR PDBsum; 4X6Z; -.
DR PDBsum; 4Y69; -.
DR PDBsum; 4Y6A; -.
DR PDBsum; 4Y6V; -.
DR PDBsum; 4Y6Z; -.
DR PDBsum; 4Y70; -.
DR PDBsum; 4Y74; -.
DR PDBsum; 4Y75; -.
DR PDBsum; 4Y77; -.
DR PDBsum; 4Y78; -.
DR PDBsum; 4Y7W; -.
DR PDBsum; 4Y7X; -.
DR PDBsum; 4Y7Y; -.
DR PDBsum; 4Y80; -.
DR PDBsum; 4Y81; -.
DR PDBsum; 4Y82; -.
DR PDBsum; 4Y84; -.
DR PDBsum; 4Y8G; -.
DR PDBsum; 4Y8H; -.
DR PDBsum; 4Y8I; -.
DR PDBsum; 4Y8J; -.
DR PDBsum; 4Y8K; -.
DR PDBsum; 4Y8L; -.
DR PDBsum; 4Y8M; -.
DR PDBsum; 4Y8N; -.
DR PDBsum; 4Y8O; -.
DR PDBsum; 4Y8P; -.
DR PDBsum; 4Y8Q; -.
DR PDBsum; 4Y8R; -.
DR PDBsum; 4Y8S; -.
DR PDBsum; 4Y8T; -.
DR PDBsum; 4Y8U; -.
DR PDBsum; 4Y9Y; -.
DR PDBsum; 4Y9Z; -.
DR PDBsum; 4YA0; -.
DR PDBsum; 4YA1; -.
DR PDBsum; 4YA2; -.
DR PDBsum; 4YA3; -.
DR PDBsum; 4YA4; -.
DR PDBsum; 4YA5; -.
DR PDBsum; 4YA7; -.
DR PDBsum; 4YA9; -.
DR PDBsum; 4Z1L; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5AHJ; -.
DR PDBsum; 5BOU; -.
DR PDBsum; 5BXL; -.
DR PDBsum; 5BXN; -.
DR PDBsum; 5CGF; -.
DR PDBsum; 5CGG; -.
DR PDBsum; 5CGH; -.
DR PDBsum; 5CGI; -.
DR PDBsum; 5CZ4; -.
DR PDBsum; 5CZ5; -.
DR PDBsum; 5CZ6; -.
DR PDBsum; 5CZ7; -.
DR PDBsum; 5CZ8; -.
DR PDBsum; 5CZ9; -.
DR PDBsum; 5CZA; -.
DR PDBsum; 5D0S; -.
DR PDBsum; 5D0T; -.
DR PDBsum; 5D0V; -.
DR PDBsum; 5D0W; -.
DR PDBsum; 5D0X; -.
DR PDBsum; 5D0Z; -.
DR PDBsum; 5DKI; -.
DR PDBsum; 5DKJ; -.
DR PDBsum; 5FG7; -.
DR PDBsum; 5FG9; -.
DR PDBsum; 5FGA; -.
DR PDBsum; 5FGD; -.
DR PDBsum; 5FGE; -.
DR PDBsum; 5FGF; -.
DR PDBsum; 5FGG; -.
DR PDBsum; 5FGH; -.
DR PDBsum; 5FGI; -.
DR PDBsum; 5FHS; -.
DR PDBsum; 5JHR; -.
DR PDBsum; 5JHS; -.
DR PDBsum; 5L52; -.
DR PDBsum; 5L54; -.
DR PDBsum; 5L55; -.
DR PDBsum; 5L5A; -.
DR PDBsum; 5L5B; -.
DR PDBsum; 5L5D; -.
DR PDBsum; 5L5E; -.
DR PDBsum; 5L5F; -.
DR PDBsum; 5L5H; -.
DR PDBsum; 5L5I; -.
DR PDBsum; 5L5J; -.
DR PDBsum; 5L5O; -.
DR PDBsum; 5L5P; -.
DR PDBsum; 5L5Q; -.
DR PDBsum; 5L5R; -.
DR PDBsum; 5L5S; -.
DR PDBsum; 5L5T; -.
DR PDBsum; 5L5U; -.
DR PDBsum; 5L5V; -.
DR PDBsum; 5L5W; -.
DR PDBsum; 5L5X; -.
DR PDBsum; 5L5Y; -.
DR PDBsum; 5L5Z; -.
DR PDBsum; 5L60; -.
DR PDBsum; 5L61; -.
DR PDBsum; 5L62; -.
DR PDBsum; 5L63; -.
DR PDBsum; 5L64; -.
DR PDBsum; 5L65; -.
DR PDBsum; 5L66; -.
DR PDBsum; 5L67; -.
DR PDBsum; 5L68; -.
DR PDBsum; 5L69; -.
DR PDBsum; 5L6A; -.
DR PDBsum; 5L6B; -.
DR PDBsum; 5L6C; -.
DR PDBsum; 5LAI; -.
DR PDBsum; 5LAJ; -.
DR PDBsum; 5LTT; -.
DR PDBsum; 5M2B; -.
DR PDBsum; 5MP9; -.
DR PDBsum; 5MPA; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5NIF; -.
DR PDBsum; 5WVI; -.
DR PDBsum; 5WVK; -.
DR PDBsum; 6EF0; -.
DR PDBsum; 6EF1; -.
DR PDBsum; 6EF2; -.
DR PDBsum; 6EF3; -.
DR PDBsum; 6FVT; -.
DR PDBsum; 6FVU; -.
DR PDBsum; 6FVV; -.
DR PDBsum; 6FVW; -.
DR PDBsum; 6FVX; -.
DR PDBsum; 6FVY; -.
DR PDBsum; 6G7F; -.
DR PDBsum; 6G8M; -.
DR PDBsum; 6G8N; -.
DR PDBsum; 6GOP; -.
DR PDBsum; 6H39; -.
DR PDBsum; 6HTB; -.
DR PDBsum; 6HTC; -.
DR PDBsum; 6HTD; -.
DR PDBsum; 6HTP; -.
DR PDBsum; 6HTR; -.
DR PDBsum; 6HUB; -.
DR PDBsum; 6HUC; -.
DR PDBsum; 6HUQ; -.
DR PDBsum; 6HUU; -.
DR PDBsum; 6HUV; -.
DR PDBsum; 6HV3; -.
DR PDBsum; 6HV4; -.
DR PDBsum; 6HV5; -.
DR PDBsum; 6HV7; -.
DR PDBsum; 6HVA; -.
DR PDBsum; 6HVR; -.
DR PDBsum; 6HVS; -.
DR PDBsum; 6HVT; -.
DR PDBsum; 6HVU; -.
DR PDBsum; 6HVV; -.
DR PDBsum; 6HVW; -.
DR PDBsum; 6HVX; -.
DR PDBsum; 6HVY; -.
DR PDBsum; 6HW0; -.
DR PDBsum; 6HW3; -.
DR PDBsum; 6HW4; -.
DR PDBsum; 6HW5; -.
DR PDBsum; 6HW6; -.
DR PDBsum; 6HW7; -.
DR PDBsum; 6HW8; -.
DR PDBsum; 6HW9; -.
DR PDBsum; 6HWA; -.
DR PDBsum; 6HWB; -.
DR PDBsum; 6HWC; -.
DR PDBsum; 6HWD; -.
DR PDBsum; 6HWE; -.
DR PDBsum; 6HWF; -.
DR PDBsum; 6J2C; -.
DR PDBsum; 6J2N; -.
DR PDBsum; 6J2Q; -.
DR PDBsum; 6J2X; -.
DR PDBsum; 6J30; -.
DR PDBsum; 6ZOU; -.
DR PDBsum; 6ZP6; -.
DR PDBsum; 6ZP8; -.
DR PDBsum; 7LS5; -.
DR PDBsum; 7LS6; -.
DR PDBsum; 7LSX; -.
DR PDBsum; 7O2L; -.
DR PDBsum; 7QO3; -.
DR PDBsum; 7QO5; -.
DR PDBsum; 7TEJ; -.
DR PDBsum; 7TEO; -.
DR PDBsum; 8OLR; -.
DR PDBsum; 8T08; -.
DR PDBsum; 8T0M; -.
DR AlphaFoldDB; P40302; -.
DR EMDB; EMD-14082; -.
DR EMDB; EMD-14084; -.
DR EMDB; EMD-23502; -.
DR EMDB; EMD-23503; -.
DR EMDB; EMD-23508; -.
DR EMDB; EMD-25847; -.
DR EMDB; EMD-25848; -.
DR EMDB; EMD-3534; -.
DR EMDB; EMD-3535; -.
DR EMDB; EMD-3536; -.
DR EMDB; EMD-3537; -.
DR EMDB; EMD-40938; -.
DR EMDB; EMD-40944; -.
DR EMDB; EMD-4321; -.
DR EMDB; EMD-4322; -.
DR EMDB; EMD-4323; -.
DR EMDB; EMD-4324; -.
DR EMDB; EMD-6693; -.
DR EMDB; EMD-6694; -.
DR EMDB; EMD-9042; -.
DR EMDB; EMD-9043; -.
DR EMDB; EMD-9044; -.
DR EMDB; EMD-9045; -.
DR EMDB; EMD-9769; -.
DR EMDB; EMD-9770; -.
DR EMDB; EMD-9771; -.
DR EMDB; EMD-9772; -.
DR EMDB; EMD-9773; -.
DR SMR; P40302; -.
DR BioGRID; 35494; 117.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1528N; -.
DR IntAct; P40302; 36.
DR MINT; P40302; -.
DR STRING; 4932.YMR314W; -.
DR MEROPS; T01.976; -.
DR iPTMnet; P40302; -.
DR UCD-2DPAGE; P40302; -.
DR MaxQB; P40302; -.
DR PaxDb; 4932-YMR314W; -.
DR PeptideAtlas; P40302; -.
DR EnsemblFungi; YMR314W_mRNA; YMR314W; YMR314W.
DR GeneID; 855362; -.
DR KEGG; sce:YMR314W; -.
DR AGR; SGD:S000004931; -.
DR SGD; S000004931; PRE5.
DR VEuPathDB; FungiDB:YMR314W; -.
DR eggNOG; KOG0863; Eukaryota.
DR GeneTree; ENSGT00550000074855; -.
DR HOGENOM; CLU_035750_8_0_1; -.
DR InParanoid; P40302; -.
DR OMA; NTQVYGK; -.
DR OrthoDB; 166567at2759; -.
DR BioCyc; YEAST:G3O-32978-MONOMER; -.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 855362; 1 hit in 10 CRISPR screens.
DR EvolutionaryTrace; P40302; -.
DR PRO; PR:P40302; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40302; Protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:SGD.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF12; PROTEASOME SUBUNIT ALPHA TYPE-1; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..234
FT /note="Proteasome subunit alpha type-6"
FT /id="PRO_0000124076"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:4FZC"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4R17"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 78..99
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4QVP"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1G0U"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:7LS6"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4QVP"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4EU2"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:1RYP"
SQ SEQUENCE 234 AA; 25604 MW; C43CBCC1C6B9E39E CRC64;
MFRNNYDGDT VTFSPTGRLF QVEYALEAIK QGSVTVGLRS NTHAVLVALK RNADELSSYQ
KKIIKCDEHM GLSLAGLAPD ARVLSNYLRQ QCNYSSLVFN RKLAVERAGH LLCDKAQKNT
QSYGGRPYGV GLLIIGYDKS GAHLLEFQPS GNVTELYGTA IGARSQGAKT YLERTLDTFI
KIDGNPDELI KAGVEAISQS LRDESLTVDN LSIAIVGKDT PFTIYDGEAV AKYI
//
