PSA7_YEAST
ID PSA7_YEAST Reviewed; 288 AA.
AC P21242; D6W357;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Probable proteasome subunit alpha type-7;
DE AltName: Full=Macropain subunit C1;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C1;
DE AltName: Full=Proteasome component C1;
DE AltName: Full=Proteinase YSCE subunit 1;
GN Name=PRE10; Synonyms=PRC1, PRS1; OrderedLocusNames=YOR362C; ORFNames=O6650;
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 [MRNA], PROTEIN SEQUENCE OF 106-135; 180-195 AND
RP 200-209, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=1697860; DOI=10.1016/s0021-9258(17)46265-x;
RA Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T.,
RA Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S.,
RA Ichihara A.;
RT "Proteasomes are essential for yeast proliferation. cDNA cloning and gene
RT disruption of two major subunits.";
RL J. Biol. Chem. 265:16604-16613(1990).
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 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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-248 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 [8]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-288 OF COMPLEX WITH THE 20S
RP PROTEASOME 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-248 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S
RP PROTEASOME 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S
RP PROTEASOME 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S
RP PROTEASOME 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 [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 5-248 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 [14]
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 P21242; P22141: PRE1; NbExp=4; IntAct=EBI-13963, EBI-13988;
CC P21242; P30656: PRE2; NbExp=3; IntAct=EBI-13963, EBI-14001;
CC P21242; P21243: SCL1; NbExp=10; IntAct=EBI-13963, EBI-13975;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- PTM: The alpha and beta forms are probably products of the same gene
CC with different post-translational modifications.
CC -!- MISCELLANEOUS: Present with 12000 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; M55436; AAA35227.1; -; mRNA.
DR EMBL; Z75270; CAA99691.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11123.1; -; Genomic_DNA.
DR PIR; S11182; SNBYC1.
DR RefSeq; NP_015007.1; NM_001183782.1.
DR PDB; 1FNT; X-ray; 3.20 A; G/U=2-288.
DR PDB; 1G0U; X-ray; 2.40 A; F/T=1-248.
DR PDB; 1G65; X-ray; 2.25 A; F/T=5-248.
DR PDB; 1JD2; X-ray; 3.00 A; 1/F=5-248.
DR PDB; 1RYP; X-ray; 1.90 A; G/U=5-248.
DR PDB; 1Z7Q; X-ray; 3.22 A; G/U=1-288.
DR PDB; 2F16; X-ray; 2.80 A; F/T=5-248.
DR PDB; 2FAK; X-ray; 2.80 A; F/T=5-248.
DR PDB; 2GPL; X-ray; 2.81 A; F/T=5-248.
DR PDB; 2ZCY; X-ray; 2.90 A; F/T=2-288.
DR PDB; 3BDM; X-ray; 2.70 A; F/T=2-288.
DR PDB; 3D29; X-ray; 2.60 A; F/T=5-248.
DR PDB; 3DY3; X-ray; 2.81 A; F/T=5-248.
DR PDB; 3DY4; X-ray; 2.80 A; F/T=5-248.
DR PDB; 3E47; X-ray; 3.00 A; F/T=5-248.
DR PDB; 3GPJ; X-ray; 2.70 A; F/T=5-248.
DR PDB; 3GPT; X-ray; 2.41 A; F/T=5-248.
DR PDB; 3GPW; X-ray; 2.50 A; F/T=5-248.
DR PDB; 3HYE; X-ray; 2.50 A; F/T=5-248.
DR PDB; 3JCO; EM; 4.80 A; G/g=1-288.
DR PDB; 3JCP; EM; 4.60 A; G/g=1-288.
DR PDB; 3MG0; X-ray; 2.68 A; F/T=5-248.
DR PDB; 3MG4; X-ray; 3.11 A; F/T=5-248.
DR PDB; 3MG6; X-ray; 2.60 A; F/T=1-248.
DR PDB; 3MG7; X-ray; 2.78 A; F/T=1-248.
DR PDB; 3MG8; X-ray; 2.59 A; F/T=1-248.
DR PDB; 3NZJ; X-ray; 2.40 A; F/T=1-288.
DR PDB; 3NZW; X-ray; 2.50 A; F/T=1-288.
DR PDB; 3NZX; X-ray; 2.70 A; F/T=1-288.
DR PDB; 3OEU; X-ray; 2.60 A; F/T=7-248.
DR PDB; 3OEV; X-ray; 2.85 A; F/T=7-248.
DR PDB; 3OKJ; X-ray; 2.70 A; F/T=5-248.
DR PDB; 3SDI; X-ray; 2.65 A; F/T=7-248.
DR PDB; 3SDK; X-ray; 2.70 A; F/T=7-248.
DR PDB; 3SHJ; X-ray; 2.80 A; F/T=5-248.
DR PDB; 3TDD; X-ray; 2.70 A; F/T=5-248.
DR PDB; 3UN4; X-ray; 3.40 A; F/T=1-288.
DR PDB; 3UN8; X-ray; 2.70 A; F/T=1-288.
DR PDB; 3WXR; X-ray; 3.15 A; G/U=13-288.
DR PDB; 4CR2; EM; 7.70 A; G=1-288.
DR PDB; 4CR3; EM; 9.30 A; G=1-288.
DR PDB; 4CR4; EM; 8.80 A; G=1-288.
DR PDB; 4EU2; X-ray; 2.51 A; G/U=5-248.
DR PDB; 4FZC; X-ray; 2.80 A; F/T=5-248.
DR PDB; 4FZG; X-ray; 3.00 A; F/T=5-248.
DR PDB; 4G4S; X-ray; 2.49 A; G=1-288.
DR PDB; 4GK7; X-ray; 2.80 A; F/T=5-248.
DR PDB; 4HNP; X-ray; 2.80 A; F/T=5-248.
DR PDB; 4HRC; X-ray; 2.80 A; F/T=5-248.
DR PDB; 4HRD; X-ray; 2.80 A; F/T=5-248.
DR PDB; 4INR; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4INT; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4INU; X-ray; 3.10 A; F/T=1-288.
DR PDB; 4J70; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4JSQ; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4JSU; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4JT0; X-ray; 3.10 A; F/T=1-288.
DR PDB; 4LQI; X-ray; 2.70 A; F/T=5-248.
DR PDB; 4LTC; X-ray; 2.50 A; F/T=2-288.
DR PDB; 4NNN; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4NNW; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4NO1; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4NO6; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4NO8; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4NO9; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4Q1S; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QBY; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QLQ; X-ray; 2.40 A; F/T=1-288.
DR PDB; 4QLS; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QLT; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QLU; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QLV; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QUX; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QUY; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QV0; X-ray; 3.10 A; F/T=1-288.
DR PDB; 4QV1; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4QV3; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QV4; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4QV5; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4QV6; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QV7; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QV8; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QV9; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QVL; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QVM; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QVN; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QVP; X-ray; 2.30 A; F/T=1-288.
DR PDB; 4QVQ; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QVV; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QVW; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QVY; X-ray; 2.51 A; F/T=1-288.
DR PDB; 4QW0; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QW1; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QW3; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QW4; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QW5; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QW6; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QW7; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4QWF; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QWG; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QWI; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QWJ; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QWK; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QWL; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QWR; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QWS; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QWU; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QWX; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QXJ; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QZ0; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QZ1; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QZ2; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4QZ3; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QZ4; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QZ5; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QZ6; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4QZ7; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4QZW; X-ray; 3.00 A; F/T=1-288.
DR PDB; 4QZX; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4QZZ; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4R00; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4R02; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4R17; X-ray; 2.10 A; F/T=1-288.
DR PDB; 4R18; X-ray; 2.40 A; F/T=1-288.
DR PDB; 4RUR; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4V7O; X-ray; 3.00 A; AL/AX/BG/BU=5-248.
DR PDB; 4X6Z; X-ray; 2.70 A; G/U=1-288.
DR PDB; 4Y69; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4Y6A; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y6V; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y6Z; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y70; X-ray; 2.40 A; F/T=1-288.
DR PDB; 4Y74; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y75; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y77; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4Y78; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y7W; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4Y7X; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y7Y; X-ray; 2.40 A; F/T=1-288.
DR PDB; 4Y80; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4Y81; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y82; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y84; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y8G; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y8H; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4Y8I; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y8J; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y8K; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y8L; X-ray; 2.40 A; F/T=1-288.
DR PDB; 4Y8M; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y8N; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y8O; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y8P; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y8Q; X-ray; 2.60 A; F/T=1-288.
DR PDB; 4Y8R; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y8S; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y8T; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Y8U; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4Y9Y; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4Y9Z; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4YA0; X-ray; 2.80 A; F/T=1-288.
DR PDB; 4YA1; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4YA2; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4YA3; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4YA4; X-ray; 2.90 A; F/T=1-288.
DR PDB; 4YA5; X-ray; 2.50 A; F/T=1-288.
DR PDB; 4YA7; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4YA9; X-ray; 2.70 A; F/T=1-288.
DR PDB; 4Z1L; X-ray; 3.00 A; F/T=1-288.
DR PDB; 5A5B; EM; 9.50 A; G=1-288.
DR PDB; 5AHJ; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5BOU; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5BXL; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5BXN; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5CGF; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5CGG; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5CGH; X-ray; 2.50 A; F/T=1-288.
DR PDB; 5CGI; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5CZ4; X-ray; 2.30 A; F/T=1-288.
DR PDB; 5CZ5; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5CZ6; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5CZ7; X-ray; 2.50 A; F/T=1-288.
DR PDB; 5CZ8; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5CZ9; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5CZA; X-ray; 2.50 A; F/T=1-288.
DR PDB; 5D0S; X-ray; 2.50 A; F/T=1-288.
DR PDB; 5D0T; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5D0V; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5D0W; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5D0X; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5D0Z; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5DKI; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5DKJ; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5FG7; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5FG9; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5FGA; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5FGD; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5FGE; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5FGF; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5FGG; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5FGH; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5FGI; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5FHS; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5JHR; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5JHS; X-ray; 3.00 A; F/T=1-288.
DR PDB; 5L52; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L54; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L55; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5A; X-ray; 2.40 A; F/T=1-288.
DR PDB; 5L5B; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L5D; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L5E; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5F; X-ray; 2.50 A; F/T=1-288.
DR PDB; 5L5H; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5L5I; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5J; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5O; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5L5P; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L5Q; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L5R; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5S; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5L5T; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5U; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5L5V; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L5W; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L5X; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L5Y; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L5Z; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L60; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L61; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L62; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L63; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L64; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L65; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5L66; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L67; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5L68; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L69; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5L6A; X-ray; 2.80 A; F/T=1-288.
DR PDB; 5L6B; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5L6C; X-ray; 2.60 A; F/T=1-288.
DR PDB; 5LAI; X-ray; 2.50 A; F/T=1-288.
DR PDB; 5LAJ; X-ray; 2.90 A; F/T=1-288.
DR PDB; 5LTT; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5M2B; X-ray; 2.70 A; F/T=1-288.
DR PDB; 5MP9; EM; 4.10 A; G/g=1-288.
DR PDB; 5MPA; EM; 4.50 A; G/g=1-288.
DR PDB; 5MPB; EM; 7.80 A; G/g=1-288.
DR PDB; 5MPC; EM; 7.70 A; G/g=1-288.
DR PDB; 5NIF; X-ray; 3.00 A; G/U=1-288.
DR PDB; 5WVI; EM; 6.30 A; G/k=1-288.
DR PDB; 5WVK; EM; 4.20 A; G/k=1-288.
DR PDB; 6EF0; EM; 4.43 A; G=3-248.
DR PDB; 6EF1; EM; 4.73 A; G=6-248.
DR PDB; 6EF2; EM; 4.27 A; G=3-248.
DR PDB; 6EF3; EM; 4.17 A; G=1-288.
DR PDB; 6FVT; EM; 4.10 A; G/g=4-248.
DR PDB; 6FVU; EM; 4.50 A; G/g=7-248.
DR PDB; 6FVV; EM; 5.40 A; G/g=7-248.
DR PDB; 6FVW; EM; 4.50 A; G/g=4-248.
DR PDB; 6FVX; EM; 4.90 A; G/g=5-248.
DR PDB; 6FVY; EM; 6.10 A; G/g=4-248.
DR PDB; 6G7F; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6G8M; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6G8N; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6GOP; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6H39; X-ray; 2.50 A; F/T=1-288.
DR PDB; 6HTB; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HTC; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HTD; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HTP; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HTR; X-ray; 2.60 A; F/T=1-288.
DR PDB; 6HUB; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6HUC; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HUQ; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HUU; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HUV; X-ray; 3.10 A; F/T=1-288.
DR PDB; 6HV3; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HV4; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HV5; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HV7; X-ray; 3.40 A; F/T=1-288.
DR PDB; 6HVA; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6HVR; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HVS; X-ray; 3.10 A; F/T=1-288.
DR PDB; 6HVT; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6HVU; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6HVV; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HVW; X-ray; 3.00 A; F/T=1-288.
DR PDB; 6HVX; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HVY; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HW0; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HW3; X-ray; 2.60 A; F/T=1-288.
DR PDB; 6HW4; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6HW5; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6HW6; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HW7; X-ray; 2.70 A; F/T=1-288.
DR PDB; 6HW8; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HW9; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HWA; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HWB; X-ray; 2.60 A; F/T=1-288.
DR PDB; 6HWC; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HWD; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6HWE; X-ray; 2.30 A; F/T=1-288.
DR PDB; 6HWF; X-ray; 2.50 A; F/T=1-288.
DR PDB; 6J2C; EM; 7.00 A; G/k=1-288.
DR PDB; 6J2N; EM; 7.50 A; G/k=1-288.
DR PDB; 6J2Q; EM; 3.80 A; G/k=1-288.
DR PDB; 6J2X; EM; 3.80 A; G/k=1-288.
DR PDB; 6J30; EM; 4.50 A; G/k=1-288.
DR PDB; 6ZOU; X-ray; 2.90 A; F/T=1-288.
DR PDB; 6ZP6; X-ray; 2.80 A; F/T=1-288.
DR PDB; 6ZP8; X-ray; 3.00 A; F/T=1-288.
DR PDB; 7LS5; EM; 2.74 A; G/U=1-288.
DR PDB; 7LS6; EM; 3.17 A; G=1-288.
DR PDB; 7LSX; EM; 3.61 A; G=1-288.
DR PDB; 7QO3; EM; 6.10 A; G/g=1-288.
DR PDB; 7QO5; EM; 6.00 A; G/g=1-288.
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; P21242; -.
DR SMR; P21242; -.
DR BioGRID; 34747; 470.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1526N; -.
DR IntAct; P21242; 33.
DR MINT; P21242; -.
DR STRING; 4932.YOR362C; -.
DR iPTMnet; P21242; -.
DR MaxQB; P21242; -.
DR PaxDb; P21242; -.
DR PRIDE; P21242; -.
DR EnsemblFungi; YOR362C_mRNA; YOR362C; YOR362C.
DR GeneID; 854544; -.
DR KEGG; sce:YOR362C; -.
DR SGD; S000005889; PRE10.
DR VEuPathDB; FungiDB:YOR362C; -.
DR eggNOG; KOG0184; Eukaryota.
DR GeneTree; ENSGT00550000074912; -.
DR HOGENOM; CLU_035750_0_1_1; -.
DR InParanoid; P21242; -.
DR OMA; SMYMHAY; -.
DR BioCyc; YEAST:G3O-33832-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; P21242; -.
DR PRO; PR:P21242; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P21242; protein.
DR GO; GO:0005737; C:cytoplasm; IC:SGD.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IC:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0003729; F:mRNA binding; 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; IPR037555; Proteasome_alpha_3.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF10; PTHR11599:SF10; 1.
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; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1697860,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..288
FT /note="Probable proteasome subunit alpha type-7"
FT /id="PRO_0000124102"
FT REGION 247..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4R18"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4INU"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4QLV"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:7LS5"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3GPT"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1JD2"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1RYP"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1RYP"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1RYP"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:1RYP"
SQ SEQUENCE 288 AA; 31536 MW; 1E51D904CF336747 CRC64;
MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV EKLITSKLLV
PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK KLYKTPIPIP AFADRLGQYV
QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM LEPSGSYWGY KGAATGKGRQ SAKAELEKLV
DHHPEGLSAR EAVKQAAKII YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI
DFAQKEINGD DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE
