位置:首页 > 蛋白库 > RBL_SYNP6
RBL_SYNP6
ID   RBL_SYNP6               Reviewed;         472 AA.
AC   P00880;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39 {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445};
GN   Name=cbbL; Synonyms=rbcA, rbcL; OrderedLocusNames=syc0130_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6307620; DOI=10.1089/dna.1983.2.121;
RA   Reichelt B.Y., Delaney S.F.;
RT   "The nucleotide sequence for the large subunit of ribulose 1,5-bisphosphate
RT   carboxylase from a unicellular cyanobacterium, Synechococcus PCC6301.";
RL   DNA 2:121-129(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CARBOXYLATION AT LYS-198.
RX   PubMed=16593333; DOI=10.1073/pnas.80.13.4050;
RA   Shinozaki K., Yamada C., Takahata N., Sugiura M.;
RT   "Molecular cloning and sequence analysis of the cyanobacterial gene for the
RT   large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:4050-4054(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shinozaki K., Sugiura M.;
RT   "Genes for the large and small subunits of ribulose-1,5-bisphosphate
RT   carboxylase/oxygenase constitute a single operon in a cyanobacterium
RT   Anacystis nidulans 6301.";
RL   Mol. Gen. Genet. 200:27-32(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 333-342.
RX   PubMed=8031129; DOI=10.1006/abbi.1994.1301;
RA   Read B.A., Tabita F.R.;
RT   "High substrate specificity factor ribulose bisphosphate
RT   carboxylase/oxygenase from eukaryotic marine algae and properties of
RT   recombinant cyanobacterial RubiSCO containing 'algal' residue
RT   modifications.";
RL   Arch. Biochem. Biophys. 312:210-218(1994).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9882445; DOI=10.1006/abbi.1998.0979;
RA   Horken K.M., Tabita F.R.;
RT   "Closely related form I ribulose bisphosphate carboxylase/oxygenase
RT   molecules that possess different CO2/O2 substrate specificities.";
RL   Arch. Biochem. Biophys. 361:183-194(1999).
RN   [7]
RP   RUBISCO FOLDING AND ASSEMBLY, AND SUBUNIT.
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17574029; DOI=10.1016/j.cell.2007.04.025;
RA   Saschenbrecker S., Bracher A., Rao K.V., Rao B.V., Hartl F.U.,
RA   Hayer-Hartl M.;
RT   "Structure and function of RbcX, an assembly chaperone for hexadecameric
RT   Rubisco.";
RL   Cell 129:1189-1200(2007).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-472 OF ACTIVATED HOLOENZYME IN
RP   COMPLEX WITH TRANSITION-STATE ANALOG 2-CABP AND MAGNESIUM, SUBUNIT, AND
RP   DISULFIDE BOND.
RX   PubMed=8245022; DOI=10.1016/s0021-9258(19)74469-x;
RA   Newman J., Gutteridge S.;
RT   "The X-ray structure of Synechococcus ribulose-bisphosphate
RT   carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.";
RL   J. Biol. Chem. 268:25876-25886(1993).
RN   [9] {ECO:0007744|PDB:1RSC}
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF INACTIVATED HOLOENZYME IN COMPLEX
RP   WITH PRODUCT ANALOG, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=7922027; DOI=10.1016/s0969-2126(00)00050-2;
RA   Newman J., Gutteridge S.;
RT   "Structure of an effector-induced inactivated state of ribulose 1,5-
RT   bisphosphate carboxylase/oxygenase: the binary complex between enzyme and
RT   xylulose 1,5-bisphosphate.";
RL   Structure 2:495-502(1994).
RN   [10] {ECO:0007744|PDB:2WVW}
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) IN COMPLEX WITH ANABAENA
RP   RBCX2, RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP   461-GLU--LEU-472; PHE-464 AND PHE-466.
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=20075914; DOI=10.1038/nature08651;
RA   Liu C., Young A.L., Starling-Windhof A., Bracher A., Saschenbrecker S.,
RA   Rao B.V., Rao K.V., Berninghausen O., Mielke T., Hartl F.U., Beckmann R.,
RA   Hayer-Hartl M.;
RT   "Coupled chaperone action in folding and assembly of hexadecameric
RT   Rubisco.";
RL   Nature 463:197-202(2010).
RN   [11] {ECO:0007744|PDB:3RG6}
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ANABAENA RBCX2,
RP   RUBISCO FOLDING AND ASSEMBLY, SUBUNIT, AND MUTAGENESIS OF GLU-49; ALA-53;
RP   67-TRP--LEU-71; GLU-106; ALA-126 AND ARG-212.
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=21765418; DOI=10.1038/nsmb.2090;
RA   Bracher A., Starling-Windhof A., Hartl F.U., Hayer-Hartl M.;
RT   "Crystal structure of a chaperone-bound assembly intermediate of form I
RT   Rubisco.";
RL   Nat. Struct. Mol. Biol. 18:875-880(2011).
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. Both reactions occur
CC       simultaneously and in competition at the same active site.
CC       {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445}.
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:0000269|PubMed:7922027,
CC         ECO:0000269|PubMed:9882445};
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:0000269|PubMed:9882445};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8245022};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8245022};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=39 uM for ribulose 1,5-bisphosphate {ECO:0000269|PubMed:9882445};
CC         KM=173 uM for CO(2) {ECO:0000269|PubMed:9882445};
CC         Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate
CC         {ECO:0000269|PubMed:9882445};
CC         Note=The CO(2)/O(2) specificity factor (tau) is 39.;
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains
CC       (PubMed:9882445, PubMed:17574029, PubMed:7922027); disulfide-linked
CC       (PubMed:8245022). The disulfide link is formed within the large subunit
CC       homodimers (PubMed:8245022, PubMed:7922027, PubMed:17574029)
CC       (Probable). The exposed C-terminus binds in a cleft in the RbcX2 (shown
CC       with endogenous and Anabaena strain CA protein) (PubMed:20075914,
CC       PubMed:21765418). RbcX2 is displaced by RbcS; as RbcX2 is removed RbcS
CC       mediates the ordering of an internal RbcL loop (Thr-64-Leu-70) in a
CC       catalytically active conformation (PubMed:17574029, PubMed:21765418)
CC       (Probable). {ECO:0000269|PubMed:17574029, ECO:0000269|PubMed:20075914,
CC       ECO:0000269|PubMed:21765418, ECO:0000269|PubMed:7922027,
CC       ECO:0000269|PubMed:8245022, ECO:0000305|PubMed:20075914,
CC       ECO:0000305|PubMed:21765418, ECO:0000305|PubMed:9882445}.
CC   -!- INTERACTION:
CC       P00880; A0A0H3K9R3: rbcX; NbExp=3; IntAct=EBI-9023246, EBI-15936812;
CC       P00880; Q44212: rbcX; Xeno; NbExp=3; IntAct=EBI-9023246, EBI-9023244;
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338}.
CC       Note=In the carboxysome RuBisCO is organized into a paracrystalline
CC       array (By similarity). This cyanobacterium makes beta-type carboxysomes
CC       (Probable). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000305}.
CC   -!- DOMAIN: Binding of RbcS probably induces a conformation change that
CC       displaces RbcX2 and triggers the final mature conformation.
CC       {ECO:0000269|PubMed:21765418, ECO:0000305|PubMed:20075914}.
CC   -!- PTM: The disulfide bond which can form in the large chain dimeric
CC       partners within the hexadecamer appears to be associated with oxidative
CC       stress and protein turnover. {ECO:0000305|PubMed:8245022}.
CC   -!- MISCELLANEOUS: RuBisCO folding and assembly commences when the nascent
CC       large subunit folds with the help of the chaperonin GroEL-GroES.
CC       Monomers require chaperone RbcX2 to assemble into RbcL8 octamers
CC       yielding RbcL8-(RbcX2)8 (PubMed:17574029) (Probable). RbcX2 is
CC       displaced by RbcS; as RbcX2 is removed RbcS mediates the ordering of an
CC       internal RbcL loop (Thr-64-Leu-70) in a catalytically active
CC       conformation (PubMed:17574029, PubMed:21765418) (Probable).
CC       {ECO:0000269|PubMed:17574029, ECO:0000269|PubMed:21765418,
CC       ECO:0000305|PubMed:20075914, ECO:0000305|PubMed:21765418}.
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:0000269|PubMed:8245022}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
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; K00486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X03220; CAA26972.1; -; Genomic_DNA.
DR   EMBL; AP008231; BAD78320.1; -; Genomic_DNA.
DR   PIR; A90941; RKYCL.
DR   RefSeq; WP_011242444.1; NC_006576.1.
DR   PDB; 1RBL; X-ray; 2.20 A; A/B/C/D/E/F/G/H=6-472.
DR   PDB; 1RSC; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-472.
DR   PDB; 2WVW; EM; 9.00 A; A/B/C/D/E/F/G/H=1-472.
DR   PDB; 3RG6; X-ray; 3.20 A; A/B=1-472.
DR   PDBsum; 1RBL; -.
DR   PDBsum; 1RSC; -.
DR   PDBsum; 2WVW; -.
DR   PDBsum; 3RG6; -.
DR   AlphaFoldDB; P00880; -.
DR   SMR; P00880; -.
DR   DIP; DIP-6210N; -.
DR   IntAct; P00880; 2.
DR   STRING; 269084.syc0130_c; -.
DR   EnsemblBacteria; BAD78320; BAD78320; syc0130_c.
DR   KEGG; syc:syc0130_c; -.
DR   eggNOG; COG1850; Bacteria.
DR   OMA; IHGHPDG; -.
DR   SABIO-RK; P00880; -.
DR   EvolutionaryTrace; P00880; -.
DR   Proteomes; UP000001175; Chromosome.
DR   GO; GO:0031470; C:carboxysome; 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   DisProt; DP02960; -.
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; Bacterial microcompartment; Calvin cycle;
KW   Carbon dioxide fixation; Carboxysome; Direct protein sequencing;
KW   Disulfide bond; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Photorespiration; Photosynthesis.
FT   CHAIN           1..472
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062651"
FT   MOTIF           461..467
FT                   /note="Interacts with RbcX2"
FT                   /evidence="ECO:0000269|PubMed:17574029"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT   ACT_SITE        291
FT                   /note="Proton acceptor"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT   BINDING         170
FT                   /ligand="substrate"
FT   BINDING         174
FT                   /ligand="substrate"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000269|PubMed:8245022"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:8245022"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:8245022"
FT   BINDING         292
FT                   /ligand="substrate"
FT   BINDING         324
FT                   /ligand="substrate"
FT   BINDING         376
FT                   /ligand="substrate"
FT   SITE            331
FT                   /note="Transition state stabilizer"
FT   MOD_RES         198
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000269|PubMed:16593333"
FT   DISULFID        244
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000269|PubMed:8245022"
FT   MUTAGEN         49
FT                   /note="E->A,C: Does not form the RbcL8-(RbcX2)8 complex."
FT                   /evidence="ECO:0000269|PubMed:21765418"
FT   MUTAGEN         53
FT                   /note="A->H: Wild-type formation of the RbcL8-(RbcX2)8
FT                   complex."
FT                   /evidence="ECO:0000269|PubMed:21765418"
FT   MUTAGEN         67..71
FT                   /note="WTDLL->ATDGA: Alters the RbcL-RbcS interface, RbcS
FT                   cannot displace RbcX2 from assembly intermediate."
FT                   /evidence="ECO:0000269|PubMed:21765418"
FT   MUTAGEN         106
FT                   /note="E->Q: Protein aggregates, forms RbcL2-RbcX(2)2
FT                   homodimer intermediate poorly."
FT                   /evidence="ECO:0000269|PubMed:21765418"
FT   MUTAGEN         126
FT                   /note="A->Y: Reduced formation of the RbcL8-(RbcX2)8
FT                   complex."
FT                   /evidence="ECO:0000269|PubMed:21765418"
FT   MUTAGEN         212
FT                   /note="R->S: Forms stable homodimer in presence of RbcX2
FT                   but does not form RbcL8 form."
FT                   /evidence="ECO:0000269|PubMed:21765418"
FT   MUTAGEN         461..472
FT                   /note="Missing: Remains bound to GroEL."
FT                   /evidence="ECO:0000269|PubMed:20075914"
FT   MUTAGEN         464
FT                   /note="F->A: Remains bound to GroEL."
FT                   /evidence="ECO:0000269|PubMed:20075914"
FT   MUTAGEN         466
FT                   /note="F->A: Remains bound to GroEL."
FT                   /evidence="ECO:0000269|PubMed:20075914"
FT   CONFLICT        38..39
FT                   /note="RF -> PV (in Ref. 1; K00486)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="A -> R (in Ref. 1; K00486)"
FT                   /evidence="ECO:0000305"
FT   HELIX           18..21
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          32..41
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           67..71
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          80..86
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           110..118
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          127..136
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           152..159
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           179..191
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           211..229
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           244..256
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          260..265
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           266..269
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           271..284
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           295..299
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           308..318
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          321..324
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           336..347
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          349..351
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           355..357
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          372..378
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           384..391
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   STRAND          396..398
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           401..404
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           410..430
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           434..448
FT                   /evidence="ECO:0007829|PDB:1RBL"
FT   HELIX           450..459
FT                   /evidence="ECO:0007829|PDB:1RBL"
SQ   SEQUENCE   472 AA;  52448 MW;  CDD8519AA9D493C9 CRC64;
     MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA GAAIAAESST
     GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY PLDLFEEGSV TNILTSIVGN
     VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH GIQVERDLLN KYGRPMLGCT IKPKLGLSAK
     NYGRAVYECL RGGLDFTKDD ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT
     APTCEEMMKR AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
     QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH IEADRSRGVF
     FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG GGTLGHPWGN APGATANRVA
     LEACVQARNE GRDLYREGGD ILREAGKWSP ELAAALDLWK EIKFEFETMD KL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024