位置:首页 > 蛋白库 > PSA5_YEAST
PSA5_YEAST
ID   PSA5_YEAST              Reviewed;         260 AA.
AC   P32379; D6VV33;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 223.
DE   RecName: Full=Proteasome subunit alpha type-5;
DE   AltName: Full=Macropain subunit PUP2;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit PUP2;
DE   AltName: Full=Proteasome component PUP2;
DE   AltName: Full=Proteinase YSCE subunit PUP2;
GN   Name=PUP2; Synonyms=DOA5; OrderedLocusNames=YGR253C; ORFNames=G9155;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1544471; DOI=10.1016/0014-5793(92)80095-x;
RA   Georgatsou E., Georgakopoulos T., Thireos G.;
RT   "Molecular cloning of an essential yeast gene encoding a proteasomal
RT   subunit.";
RL   FEBS Lett. 299:39-43(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-49.
RX   PubMed=7781614; DOI=10.1002/j.1460-2075.1995.tb07260.x;
RA   Chen P., Hochstrasser M.;
RT   "Biogenesis, structure and function of the yeast 20S proteasome.";
RL   EMBO J. 14:2620-2630(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9133741;
RX   DOI=10.1002/(sici)1097-0061(19970330)13:4<369::aid-yea81>3.0.co;2-v;
RA   Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.;
RT   "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII
RT   reveals the presence of three new open reading frames and of a tRNAThr
RT   gene.";
RL   Yeast 13:369-372(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [5]
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   [6]
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   [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-55; SER-56 AND SER-251, AND
RP   IDENTIFICATION BY 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, 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   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 9-250 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   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-250 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   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 9-250 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   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 9-250 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   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-250 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   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-250 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   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-250 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   [19]
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       P32379; Q12245: POC4; NbExp=2; IntAct=EBI-13971, EBI-2343020;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- MISCELLANEOUS: Present with 17100 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X64918; CAA46111.1; -; Genomic_DNA.
DR   EMBL; X99228; CAA67615.1; -; Genomic_DNA.
DR   EMBL; Z73038; CAA97282.1; -; Genomic_DNA.
DR   EMBL; AY558511; AAS56837.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08344.1; -; Genomic_DNA.
DR   PIR; S64585; S64585.
DR   RefSeq; NP_011769.1; NM_001181382.1.
DR   PDB; 1FNT; X-ray; 3.20 A; E/S=1-260.
DR   PDB; 1G0U; X-ray; 2.40 A; D/R=1-250.
DR   PDB; 1G65; X-ray; 2.25 A; D/R=9-250.
DR   PDB; 1JD2; X-ray; 3.00 A; D/Y=9-120, D/Y=131-250.
DR   PDB; 1RYP; X-ray; 1.90 A; E/S=9-250.
DR   PDB; 1Z7Q; X-ray; 3.22 A; E/S=1-260.
DR   PDB; 2F16; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 2FAK; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 2GPL; X-ray; 2.81 A; D/R=9-250.
DR   PDB; 2Z5C; X-ray; 2.90 A; C/F=1-260.
DR   PDB; 2ZCY; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 3BDM; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 3D29; X-ray; 2.60 A; D/R=9-250.
DR   PDB; 3DY3; X-ray; 2.81 A; D/R=9-250.
DR   PDB; 3DY4; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 3E47; X-ray; 3.00 A; D/R=9-250.
DR   PDB; 3GPJ; X-ray; 2.70 A; D/R=9-250.
DR   PDB; 3GPT; X-ray; 2.41 A; D/R=9-250.
DR   PDB; 3GPW; X-ray; 2.50 A; D/R=9-250.
DR   PDB; 3HYE; X-ray; 2.50 A; D/R=9-250.
DR   PDB; 3JCO; EM; 4.80 A; E/e=1-260.
DR   PDB; 3JCP; EM; 4.60 A; E/e=1-260.
DR   PDB; 3MG0; X-ray; 2.68 A; D/R=9-250.
DR   PDB; 3MG4; X-ray; 3.11 A; D/R=9-250.
DR   PDB; 3MG6; X-ray; 2.60 A; D/R=1-250.
DR   PDB; 3MG7; X-ray; 2.78 A; D/R=1-250.
DR   PDB; 3MG8; X-ray; 2.59 A; D/R=1-250.
DR   PDB; 3NZJ; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 3NZW; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 3NZX; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 3OEU; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 3OEV; X-ray; 2.85 A; D/R=1-260.
DR   PDB; 3OKJ; X-ray; 2.70 A; D/R=9-250.
DR   PDB; 3SDI; X-ray; 2.65 A; D/R=1-260.
DR   PDB; 3SDK; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 3SHJ; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 3TDD; X-ray; 2.70 A; D/R=9-250.
DR   PDB; 3UN4; X-ray; 3.40 A; D/R=1-260.
DR   PDB; 3UN8; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 3WXR; X-ray; 3.15 A; E/S=1-260.
DR   PDB; 4CR2; EM; 7.70 A; E=1-260.
DR   PDB; 4CR3; EM; 9.30 A; E=1-260.
DR   PDB; 4CR4; EM; 8.80 A; E=1-260.
DR   PDB; 4EU2; X-ray; 2.51 A; E/S=9-250.
DR   PDB; 4FZC; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 4FZG; X-ray; 3.00 A; D/R=9-250.
DR   PDB; 4G4S; X-ray; 2.49 A; E=1-260.
DR   PDB; 4GK7; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 4HNP; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 4HRC; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 4HRD; X-ray; 2.80 A; D/R=9-250.
DR   PDB; 4INR; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4INT; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4INU; X-ray; 3.10 A; D/R=1-260.
DR   PDB; 4J70; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4JSQ; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4JSU; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4JT0; X-ray; 3.10 A; D/R=1-260.
DR   PDB; 4LQI; X-ray; 2.70 A; D/R=9-250.
DR   PDB; 4LTC; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4NNN; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4NNW; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4NO1; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4NO6; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4NO8; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4NO9; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4Q1S; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QBY; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QLQ; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 4QLS; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QLT; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QLU; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QLV; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QUX; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QUY; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QV0; X-ray; 3.10 A; D/R=1-260.
DR   PDB; 4QV1; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4QV3; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QV4; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4QV5; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4QV6; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QV7; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QV8; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QV9; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QVL; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QVM; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QVN; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QVP; X-ray; 2.30 A; D/R=1-260.
DR   PDB; 4QVQ; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QVV; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QVW; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QVY; X-ray; 2.51 A; D/R=1-260.
DR   PDB; 4QW0; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QW1; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QW3; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QW4; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QW5; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QW6; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QW7; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4QWF; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QWG; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QWI; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QWJ; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QWK; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QWL; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QWR; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QWS; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QWU; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QWX; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QXJ; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QZ0; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QZ1; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QZ2; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4QZ3; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QZ4; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QZ5; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QZ6; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4QZ7; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4QZW; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 4QZX; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4QZZ; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4R00; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4R02; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4R17; X-ray; 2.10 A; D/R=1-260.
DR   PDB; 4R18; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 4RUR; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4V7O; X-ray; 3.00 A; AJ/AV/BE/BS=1-250.
DR   PDB; 4X6Z; X-ray; 2.70 A; E/S=1-260.
DR   PDB; 4Y69; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4Y6A; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y6V; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y6Z; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y70; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 4Y74; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y75; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y77; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4Y78; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y7W; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4Y7X; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y7Y; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 4Y80; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4Y81; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y82; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y84; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y8G; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y8H; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4Y8I; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y8J; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y8K; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y8L; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 4Y8M; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y8N; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y8O; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y8P; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y8Q; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 4Y8R; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y8S; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y8T; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Y8U; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4Y9Y; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4Y9Z; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4YA0; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 4YA1; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4YA2; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4YA3; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4YA4; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 4YA5; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 4YA7; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4YA9; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 4Z1L; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 5A5B; EM; 9.50 A; E=1-260.
DR   PDB; 5AHJ; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5BOU; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5BXL; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5BXN; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5CGF; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5CGG; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5CGH; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 5CGI; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5CZ4; X-ray; 2.30 A; D/R=1-260.
DR   PDB; 5CZ5; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5CZ6; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5CZ7; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 5CZ8; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5CZ9; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5CZA; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 5D0S; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 5D0T; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5D0V; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5D0W; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5D0X; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5D0Z; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5DKI; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5DKJ; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5FG7; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5FG9; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5FGA; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5FGD; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5FGE; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5FGF; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5FGG; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5FGH; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5FGI; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5FHS; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5JHR; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5JHS; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 5L52; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L54; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L55; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5A; X-ray; 2.40 A; D/R=1-260.
DR   PDB; 5L5B; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L5D; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L5E; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5F; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 5L5H; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5L5I; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5J; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5O; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5L5P; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L5Q; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L5R; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5S; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5L5T; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5U; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5L5V; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L5W; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L5X; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L5Y; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L5Z; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L60; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L61; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L62; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L63; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L64; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L65; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5L66; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L67; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5L68; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L69; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5L6A; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 5L6B; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5L6C; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 5LAI; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 5LAJ; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 5LTT; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5M2B; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 5MP9; EM; 4.10 A; E/e=1-260.
DR   PDB; 5MPA; EM; 4.50 A; E/e=1-260.
DR   PDB; 5MPB; EM; 7.80 A; E/e=1-260.
DR   PDB; 5MPC; EM; 7.70 A; E/e=1-260.
DR   PDB; 5NIF; X-ray; 3.00 A; E/S=1-260.
DR   PDB; 5WVI; EM; 6.30 A; E/m=1-260.
DR   PDB; 5WVK; EM; 4.20 A; E/m=1-260.
DR   PDB; 6EF0; EM; 4.43 A; E=1-249.
DR   PDB; 6EF1; EM; 4.73 A; E=9-250.
DR   PDB; 6EF2; EM; 4.27 A; E=2-248.
DR   PDB; 6EF3; EM; 4.17 A; E=1-260.
DR   PDB; 6FVT; EM; 4.10 A; E/e=7-250.
DR   PDB; 6FVU; EM; 4.50 A; E/e=2-250.
DR   PDB; 6FVV; EM; 5.40 A; E/e=7-250.
DR   PDB; 6FVW; EM; 4.50 A; E/e=6-250.
DR   PDB; 6FVX; EM; 4.90 A; E/e=7-250.
DR   PDB; 6FVY; EM; 6.10 A; E/e=6-250.
DR   PDB; 6G7F; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6G8M; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6G8N; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6GOP; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6H39; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 6HTB; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HTC; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HTD; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HTP; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HTR; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 6HUB; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6HUC; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HUQ; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HUU; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HUV; X-ray; 3.10 A; D/R=1-260.
DR   PDB; 6HV3; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HV4; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HV5; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HV7; X-ray; 3.40 A; D/R=1-260.
DR   PDB; 6HVA; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6HVR; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HVS; X-ray; 3.10 A; D/R=1-260.
DR   PDB; 6HVT; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6HVU; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6HVV; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HVW; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 6HVX; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HVY; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HW0; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HW3; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 6HW4; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6HW5; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6HW6; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HW7; X-ray; 2.70 A; D/R=1-260.
DR   PDB; 6HW8; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HW9; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HWA; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HWB; X-ray; 2.60 A; D/R=1-260.
DR   PDB; 6HWC; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HWD; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6HWE; X-ray; 2.30 A; D/R=1-260.
DR   PDB; 6HWF; X-ray; 2.50 A; D/R=1-260.
DR   PDB; 6J2C; EM; 7.00 A; E/m=1-260.
DR   PDB; 6J2N; EM; 7.50 A; E/m=1-260.
DR   PDB; 6J2Q; EM; 3.80 A; E/m=1-260.
DR   PDB; 6J2X; EM; 3.80 A; E/m=1-260.
DR   PDB; 6J30; EM; 4.50 A; E/m=1-260.
DR   PDB; 6ZOU; X-ray; 2.90 A; D/R=1-260.
DR   PDB; 6ZP6; X-ray; 2.80 A; D/R=1-260.
DR   PDB; 6ZP8; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 7LS5; EM; 2.74 A; E/S=1-260.
DR   PDB; 7LS6; EM; 3.17 A; E=1-260.
DR   PDB; 7LSX; EM; 3.61 A; E=1-260.
DR   PDB; 7O2L; X-ray; 3.00 A; D/R=1-260.
DR   PDB; 7QO3; EM; 6.10 A; E/e=1-260.
DR   PDB; 7QO5; EM; 6.00 A; E/e=1-260.
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; 2Z5C; -.
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   AlphaFoldDB; P32379; -.
DR   SMR; P32379; -.
DR   BioGRID; 33504; 191.
DR   ComplexPortal; CPX-2262; 26S Proteasome complex.
DR   DIP; DIP-1193N; -.
DR   IntAct; P32379; 13.
DR   MINT; P32379; -.
DR   STRING; 4932.YGR253C; -.
DR   iPTMnet; P32379; -.
DR   MaxQB; P32379; -.
DR   PaxDb; P32379; -.
DR   PRIDE; P32379; -.
DR   EnsemblFungi; YGR253C_mRNA; YGR253C; YGR253C.
DR   GeneID; 853168; -.
DR   KEGG; sce:YGR253C; -.
DR   SGD; S000003485; PUP2.
DR   VEuPathDB; FungiDB:YGR253C; -.
DR   eggNOG; KOG0176; Eukaryota.
DR   GeneTree; ENSGT00550000074958; -.
DR   HOGENOM; CLU_035750_4_2_1; -.
DR   InParanoid; P32379; -.
DR   OMA; FQVEYAR; -.
DR   BioCyc; YEAST:G3O-30926-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-6798695; Neutrophil degranulation.
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; P32379; -.
DR   PRO; PR:P32379; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P32379; 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: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   CDD; cd03753; proteasome_alpha_type_5; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR033812; Proteasome_alpha_type_5.
DR   InterPro; IPR000426; Proteasome_asu_N.
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; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..260
FT                   /note="Proteasome subunit alpha type-5"
FT                   /id="PRO_0000124129"
FT   MOD_RES         55
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MUTAGEN         49
FT                   /note="G->D: In DOA5-1; slight decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:7781614"
FT   CONFLICT        192
FT                   /note="T -> S (in Ref. 1; CAA46111)"
FT                   /evidence="ECO:0000305"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:4QBY"
FT   HELIX           22..31
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:1G65"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           85..103
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           109..117
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            118..121
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:4LTC"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          139..148
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            160..162
FT                   /evidence="ECO:0007829|PDB:4G4S"
FT   STRAND          164..173
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           193..207
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:1FNT"
FT   STRAND          216..223
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   TURN            224..226
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:1RYP"
FT   HELIX           233..247
FT                   /evidence="ECO:0007829|PDB:1RYP"
SQ   SEQUENCE   260 AA;  28617 MW;  E8EDEB212BF4EC6E CRC64;
     MFLTRSEYDR GVSTFSPEGR LFQVEYSLEA IKLGSTAIGI ATKEGVVLGV EKRATSPLLE
     SDSIEKIVEI DRHIGCAMSG LTADARSMIE HARTAAVTHN LYYDEDINVE SLTQSVCDLA
     LRFGEGASGE ERLMSRPFGV ALLIAGHDAD DGYQLFHAEP SGTFYRYNAK AIGSGSEGAQ
     AELLNEWHSS LTLKEAELLV LKILKQVMEE KLDENNAQLS CITKQDGFKI YDNEKTAELI
     KELKEKEAAE SPEEADVEMS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024