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Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C7-alpha) (Multicatalytic endopeptidase complex C7) (Proteasome component C7-alpha) (Proteasome component Y8) (Proteinase YSCE subunit 7) (SCL1 suppressor protein)

 PSA1_YEAST              Reviewed;         252 AA.
P21243; D6VUC6; P15708;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
23-MAY-2018, entry version 207.
RecName: Full=Proteasome subunit alpha type-1;
EC=3.4.25.1;
AltName: Full=Macropain subunit C7-alpha;
AltName: Full=Multicatalytic endopeptidase complex C7;
AltName: Full=Proteasome component C7-alpha;
AltName: Full=Proteasome component Y8;
AltName: Full=Proteinase YSCE subunit 7;
AltName: Full=SCL1 suppressor protein;
Name=SCL1; Synonyms=PRC2, PRS2; OrderedLocusNames=YGL011C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2684789; DOI=10.1016/0378-1119(89)90113-3;
Balzi E., Chen W., Capieaux E., McCusker J.H., Haber J.E., Goffeau A.;
"The suppressor gene scl1+ of Saccharomyces cerevisiae is essential
for growth.";
Gene 83:271-279(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 174-187 AND
189-198.
PubMed=1697860;
Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A.,
Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A.,
Nakanishi S., Ichihara A.;
"Proteasomes are essential for yeast proliferation. cDNA cloning and
gene disruption of two major subunits.";
J. Biol. Chem. 265:16604-16613(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=1898763; DOI=10.1128/MCB.11.1.344;
Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.;
"Molecular cloning and functional analysis of three subunits of yeast
proteasome.";
Mol. Cell. Biol. 11:344-353(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 46191 / IL125-2B;
PubMed=1882553; DOI=10.1002/yea.320070311;
Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.;
"The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1
and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals
the PDR6 gene, a new member of the genetic network controlling
pleiotropic drug resistance.";
Yeast 7:287-299(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
INTERACTION WITH CIC1.
PubMed=11500370; DOI=10.1093/emboj/20.16.4423;
Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.;
"Cic1, an adaptor protein specifically linking the 26S proteasome to
its substrate, the SCF component Cdc4.";
EMBO J. 20:4423-4431(2001).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE
20S PROTEASOME.
PubMed=9087403; DOI=10.1038/386463a0;
Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D.,
Huber R.;
"Structure of 20S proteasome from yeast at 2.4-A resolution.";
Nature 386:463-471(1997).
[14]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S
PROTEASOME.
PubMed=11081519; DOI=10.1038/35040607;
Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y.,
Wang C.C., Hill C.P.;
"Structural basis for the activation of 20S proteasomes by 11S
regulators.";
Nature 408:115-120(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE
20S PROTEASOME.
PubMed=11062564; DOI=10.1038/80992;
Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R.,
Glickman M.H., Finley D.;
"A gated channel into the proteasome core particle.";
Nat. Struct. Biol. 7:1062-1067(2000).
[16]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE
20S PROTEASOME.
PubMed=11493007; DOI=10.1006/jmbi.2001.4869;
Groll M., Koguchi Y., Huber R., Kohno J.;
"Crystal structure of the 20 S proteasome:TMC-95A complex: a non-
covalent proteasome inhibitor.";
J. Mol. Biol. 311:543-548(2001).
[17]
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE
20S PROTEASOME.
PubMed=16793518; DOI=10.1016/j.chembiol.2006.04.005;
Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.;
"TMC-95-based inhibitor design provides evidence for the catalytic
versatility of the proteasome.";
Chem. Biol. 13:607-614(2006).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE
20S PROTEASOME.
PubMed=16608349; DOI=10.1021/ja058320b;
Groll M., Huber R., Potts B.C.M.;
"Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047)
in complex with the 20S proteasome reveal important consequences of
beta-lactone ring opening and a mechanism for irreversible binding.";
J. Am. Chem. Soc. 128:5136-5141(2006).
[19]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE
20S PROTEASOME.
PubMed=16531229; DOI=10.1016/j.str.2005.11.019;
Groll M., Berkers C.R., Ploegh H.L., Ovaa H.;
"Crystal structure of the boronic acid-based proteasome inhibitor
bortezomib in complex with the yeast 20S proteasome.";
Structure 14:451-456(2006).
[20]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 IN COMPLEX WITH THE
PROTEASOME.
PubMed=20227375; DOI=10.1016/j.molcel.2010.02.002;
Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.;
"Structure of a Blm10 complex reveals common mechanisms for proteasome
binding and gate opening.";
Mol. Cell 37:728-735(2010).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S
PROTEASOME.
PubMed=22927375; DOI=10.1073/pnas.1213333109;
Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G.,
Sakata E., Nickell S., Plitzko J.M., Villa E., Baumeister W.,
Forster F.;
"Near-atomic resolution structural model of the yeast 26S
proteasome.";
Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012).
-!- FUNCTION: The proteasome degrades poly-ubiquitinated proteins in
the cytoplasm and in the nucleus. It is essential for the
regulated turnover of proteins and for the removal of misfolded
proteins. The proteasome is a multicatalytic proteinase complex
that is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. It has an ATP-dependent proteolytic activity.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000255|PROSITE-ProRule:PRU00808}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is composed
of 28 subunits that are arranged in four stacked rings, resulting
in a barrel-shaped structure. The two end rings are each formed by
seven alpha subunits, and the two central rings are each formed by
seven beta subunits. The catalytic chamber with the active sites
is on the inside of the barrel. Interacts with CIC1.
{ECO:0000269|PubMed:11500370, ECO:0000269|PubMed:20227375}.
-!- INTERACTION:
P21242:PRE10; NbExp=9; IntAct=EBI-13975, EBI-13963;
P30656:PRE2; NbExp=7; IntAct=EBI-13975, EBI-14001;
P23639:PRE8; NbExp=7; IntAct=EBI-13975, EBI-13959;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 15200 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
-!- SEQUENCE CAUTION:
Sequence=AAA35020.1; Type=Frameshift; Positions=26; Evidence={ECO:0000305};
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EMBL; M31430; AAA35020.1; ALT_FRAME; Genomic_DNA.
EMBL; X56971; CAA40292.1; -; Genomic_DNA.
EMBL; M55440; AAA35228.1; -; mRNA.
EMBL; M63641; AAA34909.1; -; Genomic_DNA.
EMBL; X56732; CAA40056.1; -; Genomic_DNA.
EMBL; S58126; AAD13894.1; -; Genomic_DNA.
EMBL; Z72533; CAA96711.1; -; Genomic_DNA.
EMBL; BK006941; DAA08087.1; -; Genomic_DNA.
PIR; S11199; SNBYS1.
RefSeq; NP_011504.3; NM_001180876.3.
PDB; 1FNT; X-ray; 3.20 A; A/O=1-252.
PDB; 1G0U; X-ray; 2.40 A; G/U=1-252.
PDB; 1G65; X-ray; 2.25 A; G/U=10-252.
PDB; 1JD2; X-ray; 3.00 A; 2/G=10-252.
PDB; 1RYP; X-ray; 1.90 A; A/O=10-252.
PDB; 1Z7Q; X-ray; 3.22 A; A/O=1-252.
PDB; 2F16; X-ray; 2.80 A; G/U=10-252.
PDB; 2FAK; X-ray; 2.80 A; G/U=10-252.
PDB; 2GPL; X-ray; 2.81 A; G/U=10-252.
PDB; 2ZCY; X-ray; 2.90 A; G/U=1-252.
PDB; 3BDM; X-ray; 2.70 A; G/U=1-252.
PDB; 3D29; X-ray; 2.60 A; G/U=12-252.
PDB; 3DY3; X-ray; 2.81 A; G/U=10-252.
PDB; 3DY4; X-ray; 2.80 A; G/U=10-252.
PDB; 3E47; X-ray; 3.00 A; G/U=10-252.
PDB; 3GPJ; X-ray; 2.70 A; G/U=10-252.
PDB; 3GPT; X-ray; 2.41 A; G/U=10-252.
PDB; 3GPW; X-ray; 2.50 A; G/U=10-252.
PDB; 3HYE; X-ray; 2.50 A; G/U=10-252.
PDB; 3JCO; EM; 4.80 A; A/a=1-252.
PDB; 3JCP; EM; 4.60 A; A/a=1-252.
PDB; 3MG0; X-ray; 2.68 A; G/U=10-252.
PDB; 3MG4; X-ray; 3.11 A; G/U=10-252.
PDB; 3MG6; X-ray; 2.60 A; G/U=1-252.
PDB; 3MG7; X-ray; 2.78 A; G/U=1-252.
PDB; 3MG8; X-ray; 2.59 A; G/U=1-252.
PDB; 3NZJ; X-ray; 2.40 A; G/U=1-252.
PDB; 3NZW; X-ray; 2.50 A; G/U=1-252.
PDB; 3NZX; X-ray; 2.70 A; G/U=1-252.
PDB; 3OEU; X-ray; 2.60 A; G/U=10-252.
PDB; 3OEV; X-ray; 2.85 A; G/U=10-252.
PDB; 3OKJ; X-ray; 2.70 A; G/U=10-252.
PDB; 3SDI; X-ray; 2.65 A; G/U=10-252.
PDB; 3SDK; X-ray; 2.70 A; G/U=10-252.
PDB; 3SHJ; X-ray; 2.80 A; G/U=10-252.
PDB; 3TDD; X-ray; 2.70 A; G/U=10-252.
PDB; 3UN4; X-ray; 3.40 A; G/U=1-252.
PDB; 3UN8; X-ray; 2.70 A; G/U=1-252.
PDB; 3WXR; X-ray; 3.15 A; A/O=1-252.
PDB; 4CR2; EM; 7.70 A; A=1-252.
PDB; 4CR3; EM; 9.30 A; A=1-252.
PDB; 4CR4; EM; 8.80 A; A=1-252.
PDB; 4EU2; X-ray; 2.51 A; A/O=10-250.
PDB; 4FZC; X-ray; 2.80 A; G/U=10-252.
PDB; 4FZG; X-ray; 3.00 A; G/U=10-252.
PDB; 4G4S; X-ray; 2.49 A; A=1-252.
PDB; 4GK7; X-ray; 2.80 A; G/U=10-252.
PDB; 4HNP; X-ray; 2.80 A; G/U=10-252.
PDB; 4HRC; X-ray; 2.80 A; G/U=10-252.
PDB; 4HRD; X-ray; 2.80 A; G/U=10-252.
PDB; 4INR; X-ray; 2.70 A; G/U=1-252.
PDB; 4INT; X-ray; 2.90 A; G/U=1-252.
PDB; 4INU; X-ray; 3.10 A; G/U=1-252.
PDB; 4J70; X-ray; 2.80 A; G/U=1-252.
PDB; 4JSQ; X-ray; 2.80 A; G/U=1-252.
PDB; 4JSU; X-ray; 2.90 A; G/U=1-252.
PDB; 4JT0; X-ray; 3.10 A; G/U=1-252.
PDB; 4LQI; X-ray; 2.70 A; G/U=10-252.
PDB; 4LTC; X-ray; 2.50 A; G/U=1-252.
PDB; 4NNN; X-ray; 2.50 A; G/U=1-252.
PDB; 4NNW; X-ray; 2.60 A; G/U=1-252.
PDB; 4NO1; X-ray; 2.50 A; G/U=1-252.
PDB; 4NO6; X-ray; 3.00 A; G/U=1-252.
PDB; 4NO8; X-ray; 2.70 A; G/U=1-252.
PDB; 4NO9; X-ray; 2.90 A; G/U=1-252.
PDB; 4Q1S; X-ray; 2.60 A; G/U=1-252.
PDB; 4QBY; X-ray; 3.00 A; G/U=1-252.
PDB; 4QLQ; X-ray; 2.40 A; G/U=1-252.
PDB; 4QLS; X-ray; 2.80 A; G/U=1-252.
PDB; 4QLT; X-ray; 2.80 A; G/U=1-252.
PDB; 4QLU; X-ray; 2.80 A; G/U=1-252.
PDB; 4QLV; X-ray; 2.90 A; G/U=1-252.
PDB; 4QUX; X-ray; 3.00 A; G/U=1-252.
PDB; 4QUY; X-ray; 2.80 A; G/U=1-252.
PDB; 4QV0; X-ray; 3.10 A; G/U=1-252.
PDB; 4QV1; X-ray; 2.50 A; G/U=1-252.
PDB; 4QV3; X-ray; 3.00 A; G/U=1-252.
PDB; 4QV4; X-ray; 2.70 A; G/U=1-252.
PDB; 4QV5; X-ray; 2.70 A; G/U=1-252.
PDB; 4QV6; X-ray; 2.80 A; G/U=1-252.
PDB; 4QV7; X-ray; 2.60 A; G/U=1-252.
PDB; 4QV8; X-ray; 2.90 A; G/U=1-252.
PDB; 4QV9; X-ray; 2.60 A; G/U=1-252.
PDB; 4QVL; X-ray; 2.80 A; G/U=1-252.
PDB; 4QVM; X-ray; 2.80 A; G/U=1-252.
PDB; 4QVN; X-ray; 2.90 A; G/U=1-252.
PDB; 4QVP; X-ray; 2.30 A; G/U=1-252.
PDB; 4QVQ; X-ray; 2.60 A; G/U=1-252.
PDB; 4QVV; X-ray; 2.80 A; G/U=1-252.
PDB; 4QVW; X-ray; 3.00 A; G/U=1-252.
PDB; 4QVY; X-ray; 2.51 A; G/U=1-252.
PDB; 4QW0; X-ray; 2.90 A; G/U=1-252.
PDB; 4QW1; X-ray; 2.90 A; G/U=1-252.
PDB; 4QW3; X-ray; 2.90 A; G/U=1-252.
PDB; 4QW4; X-ray; 2.80 A; G/U=1-252.
PDB; 4QW5; X-ray; 3.00 A; G/U=1-252.
PDB; 4QW6; X-ray; 2.90 A; G/U=1-252.
PDB; 4QW7; X-ray; 2.70 A; G/U=1-252.
PDB; 4QWF; X-ray; 3.00 A; G/U=1-252.
PDB; 4QWG; X-ray; 2.60 A; G/U=1-252.
PDB; 4QWI; X-ray; 2.60 A; G/U=1-252.
PDB; 4QWJ; X-ray; 2.90 A; G/U=1-252.
PDB; 4QWK; X-ray; 2.80 A; G/U=1-252.
PDB; 4QWL; X-ray; 2.60 A; G/U=1-252.
PDB; 4QWR; X-ray; 2.90 A; G/U=1-252.
PDB; 4QWS; X-ray; 3.00 A; G/U=1-252.
PDB; 4QWU; X-ray; 3.00 A; G/U=1-252.
PDB; 4QWX; X-ray; 2.90 A; G/U=1-252.
PDB; 4QXJ; X-ray; 2.80 A; G/U=1-252.
PDB; 4QZ0; X-ray; 3.00 A; G/U=1-252.
PDB; 4QZ1; X-ray; 3.00 A; G/U=1-252.
PDB; 4QZ2; X-ray; 2.70 A; G/U=1-252.
PDB; 4QZ3; X-ray; 2.80 A; G/U=1-252.
PDB; 4QZ4; X-ray; 3.00 A; G/U=1-252.
PDB; 4QZ5; X-ray; 2.80 A; G/U=1-252.
PDB; 4QZ6; X-ray; 2.90 A; G/U=1-252.
PDB; 4QZ7; X-ray; 2.80 A; G/U=1-252.
PDB; 4QZW; X-ray; 3.00 A; G/U=1-252.
PDB; 4QZX; X-ray; 2.60 A; G/U=1-252.
PDB; 4QZZ; X-ray; 2.90 A; G/U=1-252.
PDB; 4R00; X-ray; 2.80 A; G/U=1-252.
PDB; 4R02; X-ray; 2.50 A; G/U=1-252.
PDB; 4R17; X-ray; 2.10 A; G/U=1-252.
PDB; 4R18; X-ray; 2.40 A; G/U=1-252.
PDB; 4RUR; X-ray; 2.50 A; G/U=1-252.
PDB; 4V7O; X-ray; 3.00 A; AA/AC/BA/BO=10-252.
PDB; 4X6Z; X-ray; 2.70 A; A/O=1-252.
PDB; 4Y69; X-ray; 2.90 A; G/U=1-252.
PDB; 4Y6A; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y6V; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y6Z; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y70; X-ray; 2.40 A; G/U=1-252.
PDB; 4Y74; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y75; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y77; X-ray; 2.50 A; G/U=1-252.
PDB; 4Y78; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y7W; X-ray; 2.50 A; G/U=1-252.
PDB; 4Y7X; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y7Y; X-ray; 2.40 A; G/U=1-252.
PDB; 4Y80; X-ray; 2.50 A; G/U=1-252.
PDB; 4Y81; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y82; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y84; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y8G; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y8H; X-ray; 2.50 A; G/U=1-252.
PDB; 4Y8I; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y8J; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y8K; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y8L; X-ray; 2.40 A; G/U=1-252.
PDB; 4Y8M; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y8N; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y8O; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y8P; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y8Q; X-ray; 2.60 A; G/U=1-252.
PDB; 4Y8R; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y8S; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y8T; X-ray; 2.70 A; G/U=1-252.
PDB; 4Y8U; X-ray; 2.90 A; G/U=1-252.
PDB; 4Y9Y; X-ray; 2.80 A; G/U=1-252.
PDB; 4Y9Z; X-ray; 2.80 A; G/U=1-252.
PDB; 4YA0; X-ray; 2.80 A; G/U=1-252.
PDB; 4YA1; X-ray; 2.90 A; G/U=1-252.
PDB; 4YA2; X-ray; 2.70 A; G/U=1-252.
PDB; 4YA3; X-ray; 2.70 A; G/U=1-252.
PDB; 4YA4; X-ray; 2.90 A; G/U=1-252.
PDB; 4YA5; X-ray; 2.50 A; G/U=1-252.
PDB; 4YA7; X-ray; 2.70 A; G/U=1-252.
PDB; 4YA9; X-ray; 2.70 A; G/U=1-252.
PDB; 4Z1L; X-ray; 3.00 A; G/U=1-252.
PDB; 5A5B; EM; 9.50 A; A=1-252.
PDB; 5AHJ; X-ray; 2.80 A; G/U=1-252.
PDB; 5BOU; X-ray; 2.60 A; G/U=1-252.
PDB; 5BXL; X-ray; 2.80 A; G/U=1-252.
PDB; 5BXN; X-ray; 2.80 A; G/U=1-252.
PDB; 5CGF; X-ray; 2.80 A; G/U=1-252.
PDB; 5CGG; X-ray; 2.90 A; G/U=1-252.
PDB; 5CGH; X-ray; 2.50 A; G/U=1-252.
PDB; 5CGI; X-ray; 2.80 A; G/U=1-252.
PDB; 5CZ4; X-ray; 2.30 A; G/U=1-252.
PDB; 5CZ5; X-ray; 2.80 A; G/U=1-252.
PDB; 5CZ6; X-ray; 2.70 A; G/U=1-252.
PDB; 5CZ7; X-ray; 2.50 A; G/U=1-252.
PDB; 5CZ8; X-ray; 2.80 A; G/U=1-252.
PDB; 5CZ9; X-ray; 2.90 A; G/U=1-252.
PDB; 5CZA; X-ray; 2.50 A; G/U=1-252.
PDB; 5D0S; X-ray; 2.50 A; G/U=1-252.
PDB; 5D0T; X-ray; 2.60 A; G/U=1-252.
PDB; 5D0V; X-ray; 2.90 A; G/U=1-252.
PDB; 5D0W; X-ray; 2.80 A; G/U=1-252.
PDB; 5D0X; X-ray; 2.60 A; G/U=1-252.
PDB; 5D0Z; X-ray; 2.90 A; G/U=1-252.
PDB; 5DKI; X-ray; 2.80 A; G/U=1-252.
PDB; 5DKJ; X-ray; 2.80 A; G/U=1-252.
PDB; 5FG7; X-ray; 2.70 A; G/U=1-252.
PDB; 5FG9; X-ray; 2.60 A; G/U=1-252.
PDB; 5FGA; X-ray; 2.70 A; G/U=1-252.
PDB; 5FGD; X-ray; 2.80 A; G/U=1-252.
PDB; 5FGE; X-ray; 2.60 A; G/U=1-252.
PDB; 5FGF; X-ray; 2.60 A; G/U=1-252.
PDB; 5FGG; X-ray; 2.70 A; G/U=1-252.
PDB; 5FGH; X-ray; 2.80 A; G/U=1-252.
PDB; 5FGI; X-ray; 2.90 A; G/U=1-252.
PDB; 5FHS; X-ray; 2.70 A; G/U=1-252.
PDB; 5JHR; X-ray; 2.90 A; G/U=1-252.
PDB; 5JHS; X-ray; 3.00 A; G/U=1-252.
PDB; 5L52; X-ray; 2.70 A; G/U=1-252.
PDB; 5L54; X-ray; 2.80 A; G/U=1-252.
PDB; 5L55; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5A; X-ray; 2.40 A; G/U=1-252.
PDB; 5L5B; X-ray; 2.80 A; G/U=1-252.
PDB; 5L5D; X-ray; 2.80 A; G/U=1-252.
PDB; 5L5E; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5F; X-ray; 2.50 A; G/U=1-252.
PDB; 5L5H; X-ray; 2.60 A; G/U=1-252.
PDB; 5L5I; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5J; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5O; X-ray; 2.60 A; G/U=1-252.
PDB; 5L5P; X-ray; 2.80 A; G/U=1-252.
PDB; 5L5Q; X-ray; 2.80 A; G/U=1-252.
PDB; 5L5R; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5S; X-ray; 2.60 A; G/U=1-252.
PDB; 5L5T; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5U; X-ray; 2.60 A; G/U=1-252.
PDB; 5L5V; X-ray; 2.70 A; G/U=1-252.
PDB; 5L5W; X-ray; 2.80 A; G/U=1-252.
PDB; 5L5X; X-ray; 2.90 A; G/U=1-252.
PDB; 5L5Y; X-ray; 2.70 A; G/U=1-252.
PDB; 5L5Z; X-ray; 2.70 A; G/U=1-252.
PDB; 5L60; X-ray; 2.70 A; G/U=1-252.
PDB; 5L61; X-ray; 2.80 A; G/U=1-252.
PDB; 5L62; X-ray; 2.80 A; G/U=1-252.
PDB; 5L63; X-ray; 2.70 A; G/U=1-252.
PDB; 5L64; X-ray; 2.70 A; G/U=1-252.
PDB; 5L65; X-ray; 2.90 A; G/U=1-252.
PDB; 5L66; X-ray; 2.80 A; G/U=1-252.
PDB; 5L67; X-ray; 2.60 A; G/U=1-252.
PDB; 5L68; X-ray; 2.80 A; G/U=1-252.
PDB; 5L69; X-ray; 2.70 A; G/U=1-252.
PDB; 5L6A; X-ray; 2.80 A; G/U=1-252.
PDB; 5L6B; X-ray; 2.60 A; G/U=1-252.
PDB; 5L6C; X-ray; 2.60 A; G/U=1-252.
PDB; 5LAI; X-ray; 2.50 A; G/U=1-252.
PDB; 5LAJ; X-ray; 2.90 A; G/U=1-252.
PDB; 5LTT; X-ray; 2.70 A; G/U=1-252.
PDB; 5M2B; X-ray; 2.70 A; G/U=1-252.
PDB; 5MP9; EM; 4.10 A; A/a=1-252.
PDB; 5MPA; EM; 4.50 A; A/a=1-252.
PDB; 5MPB; EM; 7.80 A; A/a=1-252.
PDB; 5MPC; EM; 7.70 A; A/a=1-252.
PDB; 5NIF; X-ray; 3.00 A; A/O=1-252.
PDB; 5WVI; EM; 6.30 A; A/c=1-252.
PDB; 5WVK; EM; 4.20 A; A/c=1-252.
PDBsum; 1FNT; -.
PDBsum; 1G0U; -.
PDBsum; 1G65; -.
PDBsum; 1JD2; -.
PDBsum; 1RYP; -.
PDBsum; 1Z7Q; -.
PDBsum; 2F16; -.
PDBsum; 2FAK; -.
PDBsum; 2GPL; -.
PDBsum; 2ZCY; -.
PDBsum; 3BDM; -.
PDBsum; 3D29; -.
PDBsum; 3DY3; -.
PDBsum; 3DY4; -.
PDBsum; 3E47; -.
PDBsum; 3GPJ; -.
PDBsum; 3GPT; -.
PDBsum; 3GPW; -.
PDBsum; 3HYE; -.
PDBsum; 3JCO; -.
PDBsum; 3JCP; -.
PDBsum; 3MG0; -.
PDBsum; 3MG4; -.
PDBsum; 3MG6; -.
PDBsum; 3MG7; -.
PDBsum; 3MG8; -.
PDBsum; 3NZJ; -.
PDBsum; 3NZW; -.
PDBsum; 3NZX; -.
PDBsum; 3OEU; -.
PDBsum; 3OEV; -.
PDBsum; 3OKJ; -.
PDBsum; 3SDI; -.
PDBsum; 3SDK; -.
PDBsum; 3SHJ; -.
PDBsum; 3TDD; -.
PDBsum; 3UN4; -.
PDBsum; 3UN8; -.
PDBsum; 3WXR; -.
PDBsum; 4CR2; -.
PDBsum; 4CR3; -.
PDBsum; 4CR4; -.
PDBsum; 4EU2; -.
PDBsum; 4FZC; -.
PDBsum; 4FZG; -.
PDBsum; 4G4S; -.
PDBsum; 4GK7; -.
PDBsum; 4HNP; -.
PDBsum; 4HRC; -.
PDBsum; 4HRD; -.
PDBsum; 4INR; -.
PDBsum; 4INT; -.
PDBsum; 4INU; -.
PDBsum; 4J70; -.
PDBsum; 4JSQ; -.
PDBsum; 4JSU; -.
PDBsum; 4JT0; -.
PDBsum; 4LQI; -.
PDBsum; 4LTC; -.
PDBsum; 4NNN; -.
PDBsum; 4NNW; -.
PDBsum; 4NO1; -.
PDBsum; 4NO6; -.
PDBsum; 4NO8; -.
PDBsum; 4NO9; -.
PDBsum; 4Q1S; -.
PDBsum; 4QBY; -.
PDBsum; 4QLQ; -.
PDBsum; 4QLS; -.
PDBsum; 4QLT; -.
PDBsum; 4QLU; -.
PDBsum; 4QLV; -.
PDBsum; 4QUX; -.
PDBsum; 4QUY; -.
PDBsum; 4QV0; -.
PDBsum; 4QV1; -.
PDBsum; 4QV3; -.
PDBsum; 4QV4; -.
PDBsum; 4QV5; -.
PDBsum; 4QV6; -.
PDBsum; 4QV7; -.
PDBsum; 4QV8; -.
PDBsum; 4QV9; -.
PDBsum; 4QVL; -.
PDBsum; 4QVM; -.
PDBsum; 4QVN; -.
PDBsum; 4QVP; -.
PDBsum; 4QVQ; -.
PDBsum; 4QVV; -.
PDBsum; 4QVW; -.
PDBsum; 4QVY; -.
PDBsum; 4QW0; -.
PDBsum; 4QW1; -.
PDBsum; 4QW3; -.
PDBsum; 4QW4; -.
PDBsum; 4QW5; -.
PDBsum; 4QW6; -.
PDBsum; 4QW7; -.
PDBsum; 4QWF; -.
PDBsum; 4QWG; -.
PDBsum; 4QWI; -.
PDBsum; 4QWJ; -.
PDBsum; 4QWK; -.
PDBsum; 4QWL; -.
PDBsum; 4QWR; -.
PDBsum; 4QWS; -.
PDBsum; 4QWU; -.
PDBsum; 4QWX; -.
PDBsum; 4QXJ; -.
PDBsum; 4QZ0; -.
PDBsum; 4QZ1; -.
PDBsum; 4QZ2; -.
PDBsum; 4QZ3; -.
PDBsum; 4QZ4; -.
PDBsum; 4QZ5; -.
PDBsum; 4QZ6; -.
PDBsum; 4QZ7; -.
PDBsum; 4QZW; -.
PDBsum; 4QZX; -.
PDBsum; 4QZZ; -.
PDBsum; 4R00; -.
PDBsum; 4R02; -.
PDBsum; 4R17; -.
PDBsum; 4R18; -.
PDBsum; 4RUR; -.
PDBsum; 4V7O; -.
PDBsum; 4X6Z; -.
PDBsum; 4Y69; -.
PDBsum; 4Y6A; -.
PDBsum; 4Y6V; -.
PDBsum; 4Y6Z; -.
PDBsum; 4Y70; -.
PDBsum; 4Y74; -.
PDBsum; 4Y75; -.
PDBsum; 4Y77; -.
PDBsum; 4Y78; -.
PDBsum; 4Y7W; -.
PDBsum; 4Y7X; -.
PDBsum; 4Y7Y; -.
PDBsum; 4Y80; -.
PDBsum; 4Y81; -.
PDBsum; 4Y82; -.
PDBsum; 4Y84; -.
PDBsum; 4Y8G; -.
PDBsum; 4Y8H; -.
PDBsum; 4Y8I; -.
PDBsum; 4Y8J; -.
PDBsum; 4Y8K; -.
PDBsum; 4Y8L; -.
PDBsum; 4Y8M; -.
PDBsum; 4Y8N; -.
PDBsum; 4Y8O; -.
PDBsum; 4Y8P; -.
PDBsum; 4Y8Q; -.
PDBsum; 4Y8R; -.
PDBsum; 4Y8S; -.
PDBsum; 4Y8T; -.
PDBsum; 4Y8U; -.
PDBsum; 4Y9Y; -.
PDBsum; 4Y9Z; -.
PDBsum; 4YA0; -.
PDBsum; 4YA1; -.
PDBsum; 4YA2; -.
PDBsum; 4YA3; -.
PDBsum; 4YA4; -.
PDBsum; 4YA5; -.
PDBsum; 4YA7; -.
PDBsum; 4YA9; -.
PDBsum; 4Z1L; -.
PDBsum; 5A5B; -.
PDBsum; 5AHJ; -.
PDBsum; 5BOU; -.
PDBsum; 5BXL; -.
PDBsum; 5BXN; -.
PDBsum; 5CGF; -.
PDBsum; 5CGG; -.
PDBsum; 5CGH; -.
PDBsum; 5CGI; -.
PDBsum; 5CZ4; -.
PDBsum; 5CZ5; -.
PDBsum; 5CZ6; -.
PDBsum; 5CZ7; -.
PDBsum; 5CZ8; -.
PDBsum; 5CZ9; -.
PDBsum; 5CZA; -.
PDBsum; 5D0S; -.
PDBsum; 5D0T; -.
PDBsum; 5D0V; -.
PDBsum; 5D0W; -.
PDBsum; 5D0X; -.
PDBsum; 5D0Z; -.
PDBsum; 5DKI; -.
PDBsum; 5DKJ; -.
PDBsum; 5FG7; -.
PDBsum; 5FG9; -.
PDBsum; 5FGA; -.
PDBsum; 5FGD; -.
PDBsum; 5FGE; -.
PDBsum; 5FGF; -.
PDBsum; 5FGG; -.
PDBsum; 5FGH; -.
PDBsum; 5FGI; -.
PDBsum; 5FHS; -.
PDBsum; 5JHR; -.
PDBsum; 5JHS; -.
PDBsum; 5L52; -.
PDBsum; 5L54; -.
PDBsum; 5L55; -.
PDBsum; 5L5A; -.
PDBsum; 5L5B; -.
PDBsum; 5L5D; -.
PDBsum; 5L5E; -.
PDBsum; 5L5F; -.
PDBsum; 5L5H; -.
PDBsum; 5L5I; -.
PDBsum; 5L5J; -.
PDBsum; 5L5O; -.
PDBsum; 5L5P; -.
PDBsum; 5L5Q; -.
PDBsum; 5L5R; -.
PDBsum; 5L5S; -.
PDBsum; 5L5T; -.
PDBsum; 5L5U; -.
PDBsum; 5L5V; -.
PDBsum; 5L5W; -.
PDBsum; 5L5X; -.
PDBsum; 5L5Y; -.
PDBsum; 5L5Z; -.
PDBsum; 5L60; -.
PDBsum; 5L61; -.
PDBsum; 5L62; -.
PDBsum; 5L63; -.
PDBsum; 5L64; -.
PDBsum; 5L65; -.
PDBsum; 5L66; -.
PDBsum; 5L67; -.
PDBsum; 5L68; -.
PDBsum; 5L69; -.
PDBsum; 5L6A; -.
PDBsum; 5L6B; -.
PDBsum; 5L6C; -.
PDBsum; 5LAI; -.
PDBsum; 5LAJ; -.
PDBsum; 5LTT; -.
PDBsum; 5M2B; -.
PDBsum; 5MP9; -.
PDBsum; 5MPA; -.
PDBsum; 5MPB; -.
PDBsum; 5MPC; -.
PDBsum; 5NIF; -.
PDBsum; 5WVI; -.
PDBsum; 5WVK; -.
ProteinModelPortal; P21243; -.
SMR; P21243; -.
BioGrid; 33235; 381.
DIP; DIP-2810N; -.
IntAct; P21243; 30.
MINT; P21243; -.
STRING; 4932.YGL011C; -.
MEROPS; T01.971; -.
iPTMnet; P21243; -.
UCD-2DPAGE; P21243; -.
MaxQB; P21243; -.
PaxDb; P21243; -.
PRIDE; P21243; -.
EnsemblFungi; YGL011C; YGL011C; YGL011C.
GeneID; 852873; -.
KEGG; sce:YGL011C; -.
EuPathDB; FungiDB:YGL011C; -.
SGD; S000002979; SCL1.
GeneTree; ENSGT00550000074807; -.
HOGENOM; HOG000091084; -.
InParanoid; P21243; -.
KO; K02730; -.
OMA; YGYEITP; -.
OrthoDB; EOG092C47D8; -.
BioCyc; YEAST:G3O-30533-MONOMER; -.
Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-SCE-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-SCE-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-SCE-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-SCE-382556; ABC-family proteins mediated transport.
Reactome; R-SCE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-68949; Orc1 removal from chromatin.
Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
EvolutionaryTrace; P21243; -.
PRO; PR:P21243; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IC:SGD.
GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IC:SGD.
GO; GO:0005634; C:nucleus; IC:SGD.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:SGD.
GO; GO:0034515; C:proteasome storage granule; IC:SGD.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:SGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:SGD.
CDD; cd03754; proteasome_alpha_type_6; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR034642; Proteasome_subunit_alpha6.
PANTHER; PTHR11599:SF11; PTHR11599:SF11; 1.
Pfam; PF00227; Proteasome; 1.
Pfam; PF10584; Proteasome_A_N; 1.
SMART; SM00948; Proteasome_A_N; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Isopeptide bond; Nucleus;
Phosphoprotein; Protease; Proteasome; Reference proteome;
Threonine protease; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 252 Proteasome subunit alpha type-1.
/FTId=PRO_0000124141.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CROSSLNK 232 232 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
HELIX 11 14 {ECO:0000244|PDB:1RYP}.
STRAND 16 18 {ECO:0000244|PDB:1RYP}.
TURN 21 23 {ECO:0000244|PDB:1JD2}.
HELIX 26 34 {ECO:0000244|PDB:1RYP}.
TURN 35 38 {ECO:0000244|PDB:1RYP}.
STRAND 42 46 {ECO:0000244|PDB:1RYP}.
STRAND 48 56 {ECO:0000244|PDB:1RYP}.
STRAND 62 64 {ECO:0000244|PDB:3D29}.
HELIX 66 68 {ECO:0000244|PDB:1RYP}.
STRAND 71 74 {ECO:0000244|PDB:1RYP}.
STRAND 76 78 {ECO:0000244|PDB:1RYP}.
STRAND 80 85 {ECO:0000244|PDB:1RYP}.
HELIX 87 108 {ECO:0000244|PDB:1RYP}.
HELIX 114 130 {ECO:0000244|PDB:1RYP}.
STRAND 131 134 {ECO:0000244|PDB:4QVP}.
STRAND 140 147 {ECO:0000244|PDB:1RYP}.
TURN 148 150 {ECO:0000244|PDB:1RYP}.
STRAND 151 157 {ECO:0000244|PDB:1RYP}.
TURN 159 161 {ECO:0000244|PDB:1G0U}.
STRAND 163 172 {ECO:0000244|PDB:1RYP}.
HELIX 175 189 {ECO:0000244|PDB:1RYP}.
STRAND 191 193 {ECO:0000244|PDB:1RYP}.
HELIX 199 214 {ECO:0000244|PDB:1RYP}.
STRAND 222 229 {ECO:0000244|PDB:1RYP}.
STRAND 232 235 {ECO:0000244|PDB:1RYP}.
HELIX 238 248 {ECO:0000244|PDB:1RYP}.
TURN 249 251 {ECO:0000244|PDB:1G65}.
SEQUENCE 252 AA; 28001 MW; 5B938C862BC8D7EB CRC64;
MSGAAAASAA GYDRHITIFS PEGRLYQVEY AFKATNQTNI NSLAVRGKDC TVVISQKKVP
DKLLDPTTVS YIFCISRTIG MVVNGPIPDA RNAALRAKAE AAEFRYKYGY DMPCDVLAKR
MANLSQIYTQ RAYMRPLGVI LTFVSVDEEL GPSIYKTDPA GYYVGYKATA TGPKQQEITT
NLENHFKKSK IDHINEESWE KVVEFAITHM IDALGTEFSK NDLEVGVATK DKFFTLSAEN
IEERLVAIAE QD


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