RBL_SPIOL
ID RBL_SPIOL Reviewed; 475 AA.
AC P00875; Q9M3L8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Flags: Precursor;
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6269077; DOI=10.1093/nar/9.14.3251;
RA Zurawski G., Perrot B., Bottomley W., Whitfeld P.R.;
RT "The structure of the gene for the large subunit of ribulose 1,5-
RT bisphosphate carboxylase from spinach chloroplast DNA.";
RL Nucleic Acids Res. 9:3251-3270(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP PROTEIN SEQUENCE OF 3-18, FUNCTION, ACETYLATION AT PRO-3, AND LACK OF
RP METHYLATION.
RX PubMed=2928307; DOI=10.1073/pnas.86.6.1855;
RA Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.;
RT "Post-translational modifications in the large subunit of ribulose
RT bisphosphate carboxylase/oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989).
RN [4]
RP PROTEIN SEQUENCE OF 8-14 AND 466-475.
RX PubMed=3422748; DOI=10.1073/pnas.85.5.1513;
RA Mulligan R.M., Houtz R.L., Tolbert N.E.;
RT "Reaction-intermediate analogue binding by ribulose bisphosphate
RT carboxylase/oxygenase causes specific changes in proteolytic sensitivity:
RT the amino-terminal residue of the large subunit is acetylated proline.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1513-1517(1988).
RN [5]
RP PROTEIN SEQUENCE OF 165-177 AND 320-339, AND ACTIVE SITE.
RX PubMed=637859; DOI=10.1016/0006-291x(78)91351-7;
RA Stringer C.D., Hartman F.C.;
RT "Sequences of two active-site peptides from spinach ribulosebisphosphate
RT carboxylase/oxygenase.";
RL Biochem. Biophys. Res. Commun. 80:1043-1048(1978).
RN [6]
RP ACTIVATION.
RA Lorimer G.H.;
RL Submitted (OCT-1982) to the PIR data bank.
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH ABSCISIC ACID.
RX PubMed=26197050; DOI=10.1371/journal.pone.0133033;
RA Galka M.M., Rajagopalan N., Buhrow L.M., Nelson K.M., Switala J.,
RA Cutler A.J., Palmer D.R., Loewen P.C., Abrams S.R., Loewen M.C.;
RT "Identification of Interactions between Abscisic Acid and Ribulose-1,5-
RT Bisphosphate Carboxylase/Oxygenase.";
RL PLoS ONE 10:e0133033-e0133033(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH TRANSITION-STATE ANALOG, AND SUBUNIT.
RX PubMed=17740342; DOI=10.1126/science.244.4905.702;
RA Knight S., Andersson I., Braenden C.-I.;
RT "Reexamination of the three-dimensional structure of the small subunit of
RT RuBisCo from higher plants.";
RL Science 244:702-705(1989).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, ACTIVE SITE, SUBUNIT,
RP AND CARBOXYLATION AT LYS-201.
RX PubMed=2118958; DOI=10.1016/s0022-2836(05)80100-7;
RA Knight S., Andersson I., Braenden C.-I.;
RT "Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from
RT spinach at 2.4-A resolution. Subunit interactions and active site.";
RL J. Mol. Biol. 215:113-160(1990).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT, AND
RP CARBOXYLATION AT LYS-201.
RX PubMed=8648644; DOI=10.1006/jmbi.1996.0310;
RA Andersson I.;
RT "Large structures at high resolution: the 1.6-A crystal structure of
RT spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-
RT carboxyarabinitol bisphosphate.";
RL J. Mol. Biol. 259:160-174(1996).
RN [11] {ECO:0007744|PDB:1RBO, ECO:0007744|PDB:1RCO}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF INACTIVE HOLOENZYME IN COMPLEX
RP WITH INHIBITORS 4-CABP AND XUBP, AND SUBUNIT.
RX PubMed=8955130; DOI=10.1074/jbc.271.51.32894;
RA Taylor T.C., Fothergill M.D., Andersson I.;
RT "A common structural basis for the inhibition of ribulose 1,5-bisphosphate
RT carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-
RT bisphosphate.";
RL J. Biol. Chem. 271:32894-32899(1996).
RN [12] {ECO:0007744|PDB:1AA1, ECO:0007744|PDB:1AUS}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP WITH 3-PHOSPHOGLYCERATE AND MAGNESIUM, SUBUNIT, AND CARBOXYLATION AT
RP LYS-201.
RX PubMed=9092835; DOI=10.1021/bi962818w;
RA Taylor T.C., Andersson I.;
RT "Structure of a product complex of spinach ribulose-1,5-bisphosphate
RT carboxylase/oxygenase.";
RL Biochemistry 36:4041-4046(1997).
RN [13] {ECO:0007744|PDB:1RCX, ECO:0007744|PDB:1RXO}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH
RP SUBSTRATE AND CALCIUM IN ACTIVATED AND INACTIVATED STATE, SUBUNIT, AND
RP CARBOXYLATION AT LYS-201.
RX PubMed=9034362; DOI=10.1006/jmbi.1996.0738;
RA Taylor T.C., Andersson I.;
RT "The structure of the complex between rubisco and its natural substrate
RT ribulose 1,5-bisphosphate.";
RL J. Mol. Biol. 265:432-444(1997).
RN [14] {ECO:0007744|PDB:1UPM, ECO:0007744|PDB:1UPP}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOLOENZYME IN COMPLEX WITH
RP TRANSITION STATE ANALOG 2-CABP AND CALCIUM, SUBUNIT, AND CARBOXYLATION AT
RP LYS-201.
RX PubMed=14596800; DOI=10.1016/j.jmb.2003.09.025;
RA Karkehabadi S., Taylor T.C., Andersson I.;
RT "Calcium supports loop closure but not catalysis in Rubisco.";
RL J. Mol. Biol. 334:65-73(2003).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate in the photorespiration process (PubMed:2928307) (Probable).
CC Both reactions occur simultaneously and in competition at the same
CC active site (Probable). Binds to abscisic acid (ABA) which has weakly
CC inhibits carboxylation and more strongly inhibits enzyme activation
CC (PubMed:26197050). {ECO:0000269|PubMed:26197050,
CC ECO:0000269|PubMed:2928307, ECO:0000305|PubMed:14596800,
CC ECO:0000305|PubMed:17740342, ECO:0000305|PubMed:2118958,
CC ECO:0000305|PubMed:8648644, ECO:0000305|PubMed:8955130,
CC ECO:0000305|PubMed:9034362, ECO:0000305|PubMed:9092835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000269|PubMed:26197050,
CC ECO:0000305|PubMed:14596800, ECO:0000305|PubMed:17740342,
CC ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:8648644,
CC ECO:0000305|PubMed:8955130, ECO:0000305|PubMed:9034362,
CC ECO:0000305|PubMed:9092835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000305|PubMed:14596800, ECO:0000305|PubMed:17740342,
CC ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:26197050,
CC ECO:0000305|PubMed:8648644, ECO:0000305|PubMed:8955130,
CC ECO:0000305|PubMed:9034362, ECO:0000305|PubMed:9092835};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2118958, ECO:0000269|PubMed:8648644,
CC ECO:0000269|PubMed:9092835};
CC Note=Binds 1 Mg(2+) ion per subunit (PubMed:2118958, PubMed:8648644,
CC PubMed:9092835). Ca(2+) can substitute but is not catalytically
CC competent (PubMed:14596800, PubMed:9034362).
CC {ECO:0000269|PubMed:14596800, ECO:0000269|PubMed:2118958,
CC ECO:0000269|PubMed:8648644, ECO:0000269|PubMed:9034362,
CC ECO:0000269|PubMed:9092835};
CC -!- ACTIVITY REGULATION: Abscisic acid (ABA) causes weak inhibition of
CC RuBisCO catalytic activity, but more potent inhibition of RuBisCO
CC activation. {ECO:0000269|PubMed:26197050}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000269|PubMed:14596800, ECO:0000269|PubMed:17740342,
CC ECO:0000269|PubMed:2118958, ECO:0000269|PubMed:8648644,
CC ECO:0000269|PubMed:8955130, ECO:0000269|PubMed:9034362,
CC ECO:0000269|PubMed:9092835}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01338}.
CC -!- PTM: The disulfide bond which can form between Cys-247 in the large
CC chain dimeric partners within the hexadecamer appears to be associated
CC with oxidative stress and protein turnover (By similarity). The
CC disulfide bonds reported in 1RBO may be the result of oxidation during
CC crystallization. {ECO:0000250|UniProtKB:P11383, ECO:0000305}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The Plant Kingdom's sloth
CC - Issue 38 of September 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/038";
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DR EMBL; V00168; CAA23473.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88737.1; -; Genomic_DNA.
DR PIR; A01094; RKSPL.
DR PIR; A28965; A28965.
DR RefSeq; NP_054944.1; NC_002202.1.
DR PDB; 1AA1; X-ray; 2.20 A; B/E/H/L=1-475.
DR PDB; 1AUS; X-ray; 2.20 A; L/M/N/O=1-475.
DR PDB; 1IR1; X-ray; 1.80 A; A/B/C/D=1-475.
DR PDB; 1RBO; X-ray; 2.30 A; B/E/H/L=1-475.
DR PDB; 1RCO; X-ray; 2.30 A; B/E/H/K/L/O/R/V=1-475.
DR PDB; 1RCX; X-ray; 2.40 A; B/E/H/K/L/O/R/V=1-475.
DR PDB; 1RXO; X-ray; 2.20 A; B/E/H/L=1-475.
DR PDB; 1UPM; X-ray; 2.30 A; B/E/H/K/L/O/R/V=1-475.
DR PDB; 1UPP; X-ray; 2.30 A; A/C/E/G=1-475.
DR PDB; 8RUC; X-ray; 1.60 A; A/C/E/G=1-475.
DR PDBsum; 1AA1; -.
DR PDBsum; 1AUS; -.
DR PDBsum; 1IR1; -.
DR PDBsum; 1RBO; -.
DR PDBsum; 1RCO; -.
DR PDBsum; 1RCX; -.
DR PDBsum; 1RXO; -.
DR PDBsum; 1UPM; -.
DR PDBsum; 1UPP; -.
DR PDBsum; 8RUC; -.
DR AlphaFoldDB; P00875; -.
DR SMR; P00875; -.
DR DIP; DIP-27641N; -.
DR IntAct; P00875; 1.
DR MINT; P00875; -.
DR STRING; 3562.P00875; -.
DR Allergome; 3814; Spi o RuBisCO.
DR iPTMnet; P00875; -.
DR PRIDE; P00875; -.
DR GeneID; 2715621; -.
DR KEGG; soe:2715621; -.
DR OrthoDB; 474428at2759; -.
DR BRENDA; 4.1.1.39; 5812.
DR EvolutionaryTrace; P00875; -.
DR PRO; PR:P00875; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR InterPro; IPR020888; RuBisCO_lsuI.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calvin cycle; Carbon dioxide fixation;
KW Chloroplast; Direct protein sequencing; Disulfide bond; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid; Reference proteome.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:2928307"
FT /id="PRO_0000031415"
FT CHAIN 3..475
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031416"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:2118958,
FT ECO:0000269|PubMed:637859, ECO:0000305|PubMed:9092835"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:637859"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX"
FT BINDING 173
FT /ligand="substrate"
FT BINDING 177
FT /ligand="substrate"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:8648644,
FT ECO:0000269|PubMed:9092835, ECO:0000305|PubMed:14596800,
FT ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:9034362"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8648644,
FT ECO:0000269|PubMed:9092835, ECO:0000305|PubMed:14596800,
FT ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:9034362"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8648644,
FT ECO:0000269|PubMed:9092835, ECO:0000305|PubMed:14596800,
FT ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:9034362"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RXO"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX"
FT BINDING 379
FT /ligand="substrate"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX, ECO:0007744|PDB:1RXO"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX, ECO:0007744|PDB:1RXO"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9034362,
FT ECO:0007744|PDB:1RCX, ECO:0007744|PDB:1RXO"
FT SITE 14
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:2928307"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:8955130"
FT MOD_RES 3
FT /note="N-acetylproline"
FT /evidence="ECO:0000269|PubMed:2928307"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:14596800,
FT ECO:0000269|PubMed:2118958, ECO:0000269|PubMed:8648644,
FT ECO:0000269|PubMed:9034362, ECO:0000269|PubMed:9092835"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 12
FT /note="E -> G (in Ref. 2; CAB88737)"
FT /evidence="ECO:0000305"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:8RUC"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1UPP"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1RBO"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 214..232
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:8RUC"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:8RUC"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:8RUC"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:8RUC"
SQ SEQUENCE 475 AA; 52740 MW; 484FFFFD36BB1238 CRC64;
MSPQTETKAS VEFKAGVKDY KLTYYTPEYE TLDTDILAAF RVSPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTNLDRY KGRCYHIEPV AGEENQYICY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL
NATAGTCEDM MKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDYTEKDRSR
GIYFTQSWVS TPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVQA RNEGRDLARE GNTIIREATK WSPELAAACE VWKEIKFEFP AMDTV
