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Database: UniProt
Entry: Q8DIQ1
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Original site: Q8DIQ1 
ID   PSBB_THEEB              Reviewed;         510 AA.
AC   Q8DIQ1; Q9F1M3;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   07-APR-2021, entry version 119.
DE   RecName: Full=Photosystem II CP47 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE   AltName: Full=PSII 47 kDa protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE   AltName: Full=Protein CP-47 {ECO:0000255|HAMAP-Rule:MF_01495};
GN   Name=psbB {ECO:0000255|HAMAP-Rule:MF_01495}; OrderedLocusNames=tlr1530;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=15653799; DOI=10.1093/pcp/pch207;
RA   Iwai M., Katoh H., Katayama M., Ikeuchi M.;
RT   "PSII-Tc protein plays an important role in dimerization of photosystem
RT   II.";
RL   Plant Cell Physiol. 45:1809-1816(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-510 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   DOI=10.1039/B406989G;
RA   Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.;
RT   "Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a
RT   closer look at the Mn-cluster.";
RL   Phys. Chem. Chem. Phys. 6:4733-4736(2004).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14764885; DOI=10.1126/science.1093087;
RA   Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT   "Architecture of the photosynthetic oxygen-evolving center.";
RL   Science 303:1831-1838(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=16355230; DOI=10.1038/nature04224;
RA   Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT   "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT   photosystem II.";
RL   Nature 438:1040-1044(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=BP-1;
RX   PubMed=19219048; DOI=10.1038/nsmb.1559;
RA   Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT   "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT   quinones, lipids, channels and chloride.";
RL   Nat. Struct. Mol. Biol. 16:334-342(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA   Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA   Zouni A.;
RT   "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT   elongatus at 3.6 A resolution.";
RL   J. Biol. Chem. 285:26255-26262(2010).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA   Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA   Muh F., Dau H., Saenger W., Zouni A.;
RT   "Structural basis of cyanobacterial photosystem II inhibition by the
RT   herbicide terbutryn.";
RL   J. Biol. Chem. 286:15964-15972(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA   Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA   Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA   Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA   DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA   Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA   Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Room temperature femtosecond X-ray diffraction of photosystem II
RT   microcrystals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=23413188; DOI=10.1126/science.1234273;
RA   Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA   Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA   Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA   Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA   Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA   Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA   Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA   Yachandra V.K., Bergmann U., Yano J.;
RT   "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT   II at room temperature.";
RL   Science 340:491-495(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 2-505 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25043005; DOI=10.1038/nature13453;
RA   Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA   Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA   Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA   Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA   Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA   Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA   Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA   Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA   Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA   Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA   Chapman H.N., Spence J.C., Fromme P.;
RT   "Serial time-resolved crystallography of photosystem II using a femtosecond
RT   X-ray laser.";
RL   Nature 513:261-265(2014).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25006873; DOI=10.1038/ncomms5371;
RA   Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA   Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA   Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA   Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA   Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA   Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA   Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT   diffraction and spectroscopy.";
RL   Nat. Commun. 5:4371-4371(2014).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII). It binds chlorophyll and helps catalyze the primary light-
CC       induced photochemical processes of PSII. PSII is a light-driven
CC       water:plastoquinone oxidoreductase, using light energy to abstract
CC       electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01495,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:25006873}.
CC   -!- COFACTOR:
CC       Note=Binds multiple chlorophylls. PSII binds additional chlorophylls,
CC       carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01495,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3};
CC   -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC       PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC       dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01495,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01495, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC       ECO:0000269|Ref.3}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01495, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
CC       ECO:0000269|Ref.3}.
CC   -!- MASS SPECTROMETRY: Mass=56485; Mass_error=108; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01495, ECO:0000305}.
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DR   EMBL; AB052566; BAB19261.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC09082.1; -; Genomic_DNA.
DR   RefSeq; NP_682320.1; NC_004113.1.
DR   RefSeq; WP_011057370.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; B/b=1-510.
DR   PDB; 1W5C; X-ray; 3.20 A; B/H=1-510.
DR   PDB; 2AXT; X-ray; 3.00 A; B/b=1-510.
DR   PDB; 3KZI; X-ray; 3.60 A; B=1-510.
DR   PDB; 4FBY; X-ray; 6.56 A; B/N=1-510.
DR   PDB; 4IXQ; X-ray; 5.70 A; B/b=1-510.
DR   PDB; 4IXR; X-ray; 5.90 A; B/b=1-510.
DR   PDB; 4PBU; X-ray; 5.00 A; B/b=2-505.
DR   PDB; 4PJ0; X-ray; 2.44 A; B/b=1-510.
DR   PDB; 4RVY; X-ray; 5.50 A; B/b=2-505.
DR   PDB; 4TNH; X-ray; 4.90 A; B/b=1-510.
DR   PDB; 4TNI; X-ray; 4.60 A; B/b=1-510.
DR   PDB; 4TNJ; X-ray; 4.50 A; B/b=1-510.
DR   PDB; 4TNK; X-ray; 5.20 A; B/b=1-510.
DR   PDB; 4V62; X-ray; 2.90 A; AB/BB=1-510.
DR   PDB; 4V82; X-ray; 3.20 A; AB/BB=1-510.
DR   PDB; 5E79; X-ray; 3.50 A; B/b=2-505.
DR   PDB; 5E7C; X-ray; 4.50 A; B/b=2-505.
DR   PDB; 5H2F; X-ray; 2.20 A; B/b=2-506.
DR   PDB; 5KAF; X-ray; 3.00 A; B/b=1-510.
DR   PDB; 5KAI; X-ray; 2.80 A; B/b=1-510.
DR   PDB; 5MX2; X-ray; 2.20 A; B/b=1-510.
DR   PDB; 5TIS; X-ray; 2.25 A; B/b=1-510.
DR   PDB; 5ZZN; X-ray; 2.10 A; B/b=2-506.
DR   PDB; 6DHE; X-ray; 2.05 A; B/b=2-506.
DR   PDB; 6DHF; X-ray; 2.08 A; B/b=2-506.
DR   PDB; 6DHG; X-ray; 2.50 A; B/b=2-506.
DR   PDB; 6DHH; X-ray; 2.20 A; B/b=2-506.
DR   PDB; 6DHO; X-ray; 2.07 A; B/b=2-506.
DR   PDB; 6DHP; X-ray; 2.04 A; B/b=2-506.
DR   PDB; 6W1O; X-ray; 2.08 A; B/b=1-506.
DR   PDB; 6W1P; X-ray; 2.26 A; B/b=1-506.
DR   PDB; 6W1Q; X-ray; 2.27 A; B/b=1-506.
DR   PDB; 6W1R; X-ray; 2.23 A; B/b=1-506.
DR   PDB; 6W1T; X-ray; 2.01 A; B/b=1-506.
DR   PDB; 6W1U; X-ray; 2.09 A; B/b=1-510.
DR   PDB; 6W1V; X-ray; 2.09 A; B/b=1-510.
DR   PDBsum; 1S5L; -.
DR   PDBsum; 1W5C; -.
DR   PDBsum; 2AXT; -.
DR   PDBsum; 3KZI; -.
DR   PDBsum; 4FBY; -.
DR   PDBsum; 4IXQ; -.
DR   PDBsum; 4IXR; -.
DR   PDBsum; 4PBU; -.
DR   PDBsum; 4PJ0; -.
DR   PDBsum; 4RVY; -.
DR   PDBsum; 4TNH; -.
DR   PDBsum; 4TNI; -.
DR   PDBsum; 4TNJ; -.
DR   PDBsum; 4TNK; -.
DR   PDBsum; 4V62; -.
DR   PDBsum; 4V82; -.
DR   PDBsum; 5E79; -.
DR   PDBsum; 5E7C; -.
DR   PDBsum; 5H2F; -.
DR   PDBsum; 5KAF; -.
DR   PDBsum; 5KAI; -.
DR   PDBsum; 5MX2; -.
DR   PDBsum; 5TIS; -.
DR   PDBsum; 5ZZN; -.
DR   PDBsum; 6DHE; -.
DR   PDBsum; 6DHF; -.
DR   PDBsum; 6DHG; -.
DR   PDBsum; 6DHH; -.
DR   PDBsum; 6DHO; -.
DR   PDBsum; 6DHP; -.
DR   PDBsum; 6W1O; -.
DR   PDBsum; 6W1P; -.
DR   PDBsum; 6W1Q; -.
DR   PDBsum; 6W1R; -.
DR   PDBsum; 6W1T; -.
DR   PDBsum; 6W1U; -.
DR   PDBsum; 6W1V; -.
DR   SMR; Q8DIQ1; -.
DR   DIP; DIP-48488N; -.
DR   IntAct; Q8DIQ1; 1.
DR   STRING; 197221.22295255; -.
DR   EnsemblBacteria; BAC09082; BAC09082; BAC09082.
DR   KEGG; tel:tlr1530; -.
DR   PATRIC; fig|197221.4.peg.1607; -.
DR   eggNOG; ENOG502Z7TN; Bacteria.
DR   OMA; MLAAIWH; -.
DR   OrthoDB; 174499at2; -.
DR   EvolutionaryTrace; Q8DIQ1; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   HAMAP; MF_01495; PSII_PsbB_CP47; 1.
DR   InterPro; IPR000932; PS_antenna-like.
DR   InterPro; IPR036001; PS_II_antenna-like_sf.
DR   InterPro; IPR017486; PSII_PsbB.
DR   PANTHER; PTHR33180; PTHR33180; 1.
DR   Pfam; PF00421; PSII; 1.
DR   SUPFAM; SSF161077; SSF161077; 1.
DR   TIGRFAMs; TIGR03039; PS_II_CP47; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chlorophyll; Chromophore; Membrane; Photosynthesis;
KW   Photosystem II; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   CHAIN           2..510
FT                   /note="Photosystem II CP47 reaction center protein"
FT                   /id="PRO_0000430806"
FT   TOPO_DOM        2..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        23..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        38..95
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        96..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        110..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        142..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        157..200
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        201..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        214..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        239..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        253..453
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        454..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        469..510
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   HELIX           5..12
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           16..44
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            50..52
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           55..57
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           63..68
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          77..79
FT                   /evidence="ECO:0007744|PDB:5H2F"
FT   STRAND          90..92
FT                   /evidence="ECO:0007744|PDB:1S5L"
FT   HELIX           93..116
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           121..123
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            126..128
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          129..131
FT                   /evidence="ECO:0007744|PDB:5KAF"
FT   HELIX           135..155
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            156..159
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          160..163
FT                   /evidence="ECO:0007744|PDB:5TIS"
FT   STRAND          166..168
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          173..175
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          177..179
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           187..190
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          192..194
FT                   /evidence="ECO:0007744|PDB:1W5C"
FT   HELIX           195..218
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           223..228
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            229..232
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           234..258
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          261..263
FT                   /evidence="ECO:0007744|PDB:1W5C"
FT   HELIX           265..268
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           272..276
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           279..293
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           298..303
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           307..312
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           315..317
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          319..321
FT                   /evidence="ECO:0007744|PDB:5MX2"
FT   HELIX           330..332
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          336..347
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          353..356
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          369..371
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          377..380
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           385..387
FT                   /evidence="ECO:0007744|PDB:2AXT"
FT   STRAND          389..391
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           392..395
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          398..404
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            405..408
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          409..411
FT                   /evidence="ECO:0007744|PDB:4PJ0"
FT   HELIX           414..424
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          427..433
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            435..438
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           447..474
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           476..478
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           488..491
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          492..498
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           502..504
FT                   /evidence="ECO:0007744|PDB:5ZZN"
SQ   SEQUENCE   510 AA;  56604 MW;  0AEEE3DB7124FB81 CRC64;
     MGLPWYRVHT VLINDPGRLI AAHLMHTALV AGWAGSMALY ELATFDPSDP VLNPMWRQGM
     FVLPFMARLG VTGSWSGWSI TGETGIDPGF WSFEGVALAH IVLSGLLFLA ACWHWVYWDL
     ELFRDPRTGE PALDLPKMFG IHLFLAGLLC FGFGAFHLTG LFGPGMWVSD PYGLTGSVQP
     VAPEWGPDGF NPYNPGGVVA HHIAAGIVGI IAGLFHILVR PPQRLYKALR MGNIETVLSS
     SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDSSYF QQEINRRVQA SLASGATLEE
     AWSAIPEKLA FYDYIGNNPA KGGLFRTGPM NKGDGIAQAW KGHAVFRNKE GEELFVRRMP
     AFFESFPVIL TDKNGVVKAD IPFRRAESKY SFEQQGVTVS FYGGELNGQT FTDPPTVKSY
     ARKAIFGEIF EFDTETLNSD GIFRTSPRGW FTFAHAVFAL LFFFGHIWHG ARTLFRDVFS
     GIDPELSPEQ VEWGFYQKVG DVTTRRKEAV
//
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