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PSA4_YEAST
ID   PSA4_YEAST              Reviewed;         254 AA.
AC   P40303; D6W229;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 219.
DE   RecName: Full=Proteasome subunit alpha type-4;
DE   AltName: Full=Macropain subunit PRE6;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit PRE6;
DE   AltName: Full=Proteasome component PRE6;
DE   AltName: Full=Proteinase YSCE subunit PRE6;
GN   Name=PRE6; OrderedLocusNames=YOL038W;
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].
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=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   PROTEIN SEQUENCE OF 112-133.
RA   Troendle N.;
RL   Thesis (1991), University of Stuttgart, Germany.
RN   [5]
RP   INTERACTION WITH CIC1.
RX   PubMed=11500370; DOI=10.1093/emboj/20.16.4423;
RA   Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.;
RT   "Cic1, an adaptor protein specifically linking the 26S proteasome to its
RT   substrate, the SCF component Cdc4.";
RL   EMBO J. 20:4423-4431(2001).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-343 OF COMPLEX WITH THE 20S
RP   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   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-243 OF COMPLEX WITH THE 20S
RP   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   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-243 OF COMPLEX WITH THE 20S
RP   PROTEASOME.
RX   PubMed=11493007; DOI=10.1006/jmbi.2001.4869;
RA   Groll M., Koguchi Y., Huber R., Kohno J.;
RT   "Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent
RT   proteasome inhibitor.";
RL   J. Mol. Biol. 311:543-548(2001).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 3-243 OF COMPLEX WITH THE 20S
RP   PROTEASOME.
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 3-243 OF COMPLEX WITH THE 20S
RP   PROTEASOME.
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 3-243 OF COMPLEX WITH THE 20S
RP   PROTEASOME.
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) OF 17-243 IN COMPLEX WITH THE
RP   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. Interacts with CIC1. {ECO:0000269|PubMed:11500370,
CC       ECO:0000269|PubMed:20227375}.
CC   -!- INTERACTION:
CC       P40303; P38779: CIC1; NbExp=5; IntAct=EBI-13980, EBI-24538;
CC       P40303; P22141: PRE1; NbExp=5; IntAct=EBI-13980, EBI-13988;
CC       P40303; P30656: PRE2; NbExp=3; IntAct=EBI-13980, EBI-14001;
CC       P40303; P38937: cut8; Xeno; NbExp=2; IntAct=EBI-13980, EBI-1152591;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 16800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; L34348; AAA34903.1; -; Genomic_DNA.
DR   EMBL; Z74780; CAA99040.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10745.1; -; Genomic_DNA.
DR   PIR; B55904; B55904.
DR   RefSeq; NP_014604.1; NM_001183292.1.
DR   PDB; 1FNT; X-ray; 3.20 A; D/R=1-254.
DR   PDB; 1G0U; X-ray; 2.40 A; C/Q=1-243.
DR   PDB; 1G65; X-ray; 2.25 A; C/Q=3-243.
DR   PDB; 1JD2; X-ray; 3.00 A; C/X=3-243.
DR   PDB; 1RYP; X-ray; 1.90 A; D/R=3-243.
DR   PDB; 1Z7Q; X-ray; 3.22 A; D/R=1-254.
DR   PDB; 2F16; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 2FAK; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 2GPL; X-ray; 2.81 A; C/Q=3-243.
DR   PDB; 2ZCY; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 3BDM; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 3D29; X-ray; 2.60 A; C/Q=3-236.
DR   PDB; 3DY3; X-ray; 2.81 A; C/Q=3-243.
DR   PDB; 3DY4; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 3E47; X-ray; 3.00 A; C/Q=3-243.
DR   PDB; 3GPJ; X-ray; 2.70 A; C/Q=3-243.
DR   PDB; 3GPT; X-ray; 2.41 A; C/Q=3-243.
DR   PDB; 3GPW; X-ray; 2.50 A; C/Q=3-243.
DR   PDB; 3HYE; X-ray; 2.50 A; C/Q=3-243.
DR   PDB; 3JCO; EM; 4.80 A; D/d=1-254.
DR   PDB; 3JCP; EM; 4.60 A; D/d=1-254.
DR   PDB; 3MG0; X-ray; 2.68 A; C/Q=3-243.
DR   PDB; 3MG4; X-ray; 3.11 A; C/Q=3-243.
DR   PDB; 3MG6; X-ray; 2.60 A; C/Q=1-243.
DR   PDB; 3MG7; X-ray; 2.78 A; C/Q=1-243.
DR   PDB; 3MG8; X-ray; 2.59 A; C/Q=1-243.
DR   PDB; 3NZJ; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 3NZW; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 3NZX; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 3OEU; X-ray; 2.60 A; C/Q=3-243.
DR   PDB; 3OEV; X-ray; 2.85 A; C/Q=3-243.
DR   PDB; 3OKJ; X-ray; 2.70 A; C/Q=3-243.
DR   PDB; 3SDI; X-ray; 2.65 A; C/Q=3-243.
DR   PDB; 3SDK; X-ray; 2.70 A; C/Q=3-243.
DR   PDB; 3SHJ; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 3TDD; X-ray; 2.70 A; C/Q=3-243.
DR   PDB; 3UN4; X-ray; 3.40 A; C/Q=1-254.
DR   PDB; 3UN8; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 3WXR; X-ray; 3.15 A; D/R=1-254.
DR   PDB; 4CR2; EM; 7.70 A; D=1-254.
DR   PDB; 4CR3; EM; 9.30 A; D=1-254.
DR   PDB; 4CR4; EM; 8.80 A; D=1-254.
DR   PDB; 4EU2; X-ray; 2.51 A; D/R=3-243.
DR   PDB; 4FZC; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 4FZG; X-ray; 3.00 A; C/Q=3-243.
DR   PDB; 4G4S; X-ray; 2.49 A; D=1-254.
DR   PDB; 4GK7; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 4HNP; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 4HRC; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 4HRD; X-ray; 2.80 A; C/Q=3-243.
DR   PDB; 4INR; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4INT; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4INU; X-ray; 3.10 A; C/Q=1-254.
DR   PDB; 4J70; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4JSQ; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4JSU; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4JT0; X-ray; 3.10 A; C/Q=1-254.
DR   PDB; 4LQI; X-ray; 2.70 A; C/Q=3-243.
DR   PDB; 4LTC; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4NNN; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4NNW; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4NO1; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4NO6; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4NO8; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4NO9; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4Q1S; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QBY; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QLQ; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 4QLS; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QLT; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QLU; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QLV; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QUX; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QUY; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QV0; X-ray; 3.10 A; C/Q=1-254.
DR   PDB; 4QV1; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4QV3; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QV4; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4QV5; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4QV6; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QV7; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QV8; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QV9; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QVL; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QVM; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QVN; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QVP; X-ray; 2.30 A; C/Q=1-254.
DR   PDB; 4QVQ; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QVV; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QVW; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QVY; X-ray; 2.51 A; C/Q=1-254.
DR   PDB; 4QW0; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QW1; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QW3; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QW4; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QW5; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QW6; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QW7; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4QWF; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QWG; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QWI; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QWJ; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QWK; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QWL; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QWR; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QWS; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QWU; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QWX; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QXJ; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QZ0; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QZ1; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QZ2; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4QZ3; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QZ4; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QZ5; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QZ6; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4QZ7; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4QZW; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 4QZX; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4QZZ; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4R00; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4R02; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4R17; X-ray; 2.10 A; C/Q=1-254.
DR   PDB; 4R18; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 4RUR; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4V7O; X-ray; 3.00 A; AI/AU/BD/BR=17-243.
DR   PDB; 4X6Z; X-ray; 2.70 A; D/R=1-254.
DR   PDB; 4Y69; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4Y6A; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y6V; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y6Z; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y70; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 4Y74; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y75; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y77; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4Y78; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y7W; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4Y7X; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y7Y; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 4Y80; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4Y81; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y82; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y84; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y8G; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y8H; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4Y8I; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y8J; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y8K; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y8L; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 4Y8M; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y8N; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y8O; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y8P; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y8Q; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 4Y8R; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y8S; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y8T; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Y8U; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4Y9Y; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4Y9Z; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4YA0; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 4YA1; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4YA2; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4YA3; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4YA4; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 4YA5; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 4YA7; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4YA9; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 4Z1L; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 5A5B; EM; 9.50 A; D=1-254.
DR   PDB; 5AHJ; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5BOU; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5BXL; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5BXN; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5CGF; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5CGG; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5CGH; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 5CGI; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5CZ4; X-ray; 2.30 A; C/Q=1-254.
DR   PDB; 5CZ5; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5CZ6; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5CZ7; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 5CZ8; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5CZ9; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5CZA; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 5D0S; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 5D0T; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5D0V; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5D0W; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5D0X; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5D0Z; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5DKI; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5DKJ; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5FG7; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5FG9; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5FGA; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5FGD; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5FGE; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5FGF; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5FGG; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5FGH; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5FGI; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5FHS; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5JHR; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5JHS; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 5L52; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L54; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L55; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5A; X-ray; 2.40 A; C/Q=1-254.
DR   PDB; 5L5B; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L5D; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L5E; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5F; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 5L5H; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5L5I; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5J; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5O; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5L5P; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L5Q; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L5R; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5S; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5L5T; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5U; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5L5V; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L5W; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L5X; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L5Y; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L5Z; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L60; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L61; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L62; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L63; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L64; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L65; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5L66; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L67; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5L68; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L69; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5L6A; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 5L6B; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5L6C; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 5LAI; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 5LAJ; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 5LTT; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5M2B; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 5MP9; EM; 4.10 A; D/d=1-254.
DR   PDB; 5MPA; EM; 4.50 A; D/d=1-254.
DR   PDB; 5MPB; EM; 7.80 A; D/d=1-254.
DR   PDB; 5MPC; EM; 7.70 A; D/d=1-254.
DR   PDB; 5NIF; X-ray; 3.00 A; D/R=1-254.
DR   PDB; 5WVI; EM; 6.30 A; D/n=1-254.
DR   PDB; 5WVK; EM; 4.20 A; D/n=1-254.
DR   PDB; 6EF0; EM; 4.43 A; D=1-242.
DR   PDB; 6EF1; EM; 4.73 A; D=9-242.
DR   PDB; 6EF2; EM; 4.27 A; D=2-242.
DR   PDB; 6EF3; EM; 4.17 A; D=1-254.
DR   PDB; 6FVT; EM; 4.10 A; D/d=4-254.
DR   PDB; 6FVU; EM; 4.50 A; D/d=4-254.
DR   PDB; 6FVV; EM; 5.40 A; D/d=4-254.
DR   PDB; 6FVW; EM; 4.50 A; D/d=3-254.
DR   PDB; 6FVX; EM; 4.90 A; D/d=3-254.
DR   PDB; 6FVY; EM; 6.10 A; D/d=3-254.
DR   PDB; 6G7F; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6G8M; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6G8N; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6GOP; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6H39; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 6HTB; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HTC; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HTD; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HTP; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HTR; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 6HUB; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6HUC; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HUQ; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HUU; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HUV; X-ray; 3.10 A; C/Q=1-254.
DR   PDB; 6HV3; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HV4; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HV5; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HV7; X-ray; 3.40 A; C/Q=1-254.
DR   PDB; 6HVA; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6HVR; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HVS; X-ray; 3.10 A; C/Q=1-254.
DR   PDB; 6HVT; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6HVU; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6HVV; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HVW; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 6HVX; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HVY; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HW0; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HW3; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 6HW4; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6HW5; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6HW6; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HW7; X-ray; 2.70 A; C/Q=1-254.
DR   PDB; 6HW8; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HW9; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HWA; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HWB; X-ray; 2.60 A; C/Q=1-254.
DR   PDB; 6HWC; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HWD; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6HWE; X-ray; 2.30 A; C/Q=1-254.
DR   PDB; 6HWF; X-ray; 2.50 A; C/Q=1-254.
DR   PDB; 6J2C; EM; 7.00 A; D/n=1-254.
DR   PDB; 6J2N; EM; 7.50 A; D/n=1-254.
DR   PDB; 6J2Q; EM; 3.80 A; D/n=1-254.
DR   PDB; 6J2X; EM; 3.80 A; D/n=1-254.
DR   PDB; 6J30; EM; 4.50 A; D/n=1-254.
DR   PDB; 6ZOU; X-ray; 2.90 A; C/Q=1-254.
DR   PDB; 6ZP6; X-ray; 2.80 A; C/Q=1-254.
DR   PDB; 6ZP8; X-ray; 3.00 A; C/Q=1-254.
DR   PDB; 7LS5; EM; 2.74 A; D/R=1-254.
DR   PDB; 7LS6; EM; 3.17 A; D=1-254.
DR   PDB; 7LSX; EM; 3.61 A; D=1-254.
DR   PDB; 7QO3; EM; 6.10 A; D/d=1-254.
DR   PDB; 7QO5; EM; 6.00 A; D/d=1-254.
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; 7QO3; -.
DR   PDBsum; 7QO5; -.
DR   AlphaFoldDB; P40303; -.
DR   SMR; P40303; -.
DR   BioGRID; 34364; 288.
DR   ComplexPortal; CPX-2262; 26S Proteasome complex.
DR   DIP; DIP-4844N; -.
DR   IntAct; P40303; 45.
DR   MINT; P40303; -.
DR   STRING; 4932.YOL038W; -.
DR   iPTMnet; P40303; -.
DR   MaxQB; P40303; -.
DR   PaxDb; P40303; -.
DR   PRIDE; P40303; -.
DR   EnsemblFungi; YOL038W_mRNA; YOL038W; YOL038W.
DR   GeneID; 854119; -.
DR   KEGG; sce:YOL038W; -.
DR   SGD; S000005398; PRE6.
DR   VEuPathDB; FungiDB:YOL038W; -.
DR   eggNOG; KOG0183; Eukaryota.
DR   GeneTree; ENSGT00940000167759; -.
DR   HOGENOM; CLU_035750_4_0_1; -.
DR   InParanoid; P40303; -.
DR   OMA; KICMLDH; -.
DR   BioCyc; YEAST:G3O-33452-MON; -.
DR   Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR   Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR   Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR   Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-SCE-8951664; Neddylation.
DR   Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   EvolutionaryTrace; P40303; -.
DR   PRO; PR:P40303; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P40303; protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
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; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 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; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Proteasome subunit alpha type-4"
FT                   /id="PRO_0000124165"
FT   REGION          235..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:1FNT"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           79..100
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           106..119
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:4G4S"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:1FNT"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:1FNT"
FT   STRAND          156..165
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           168..176
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:4QVP"
FT   HELIX           188..203
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:4R17"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           226..236
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:1RYP"
SQ   SEQUENCE   254 AA;  28439 MW;  73AEE63B836E618A CRC64;
     MSGYDRALSI FSPDGHIFQV EYALEAVKRG TCAVGVKGKN CVVLGCERRS TLKLQDTRIT
     PSKVSKIDSH VVLSFSGLNA DSRILIEKAR VEAQSHRLTL EDPVTVEYLT RYVAGVQQRY
     TQSGGVRPFG VSTLIAGFDP RDDEPKLYQT EPSGIYSSWS AQTIGRNSKT VREFLEKNYD
     RKEPPATVEE CVKLTVRSLL EVVQTGAKNI EITVVKPDSD IVALSSEEIN QYVTQIEQEK
     QEQQEQDKKK KSNH
 
 
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