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PSBB_NUPAD
ID   PSBB_NUPAD              Reviewed;         508 AA.
AC   Q4FFN0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
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};
OS   Nuphar advena (Common spatterdock) (Nuphar lutea subsp. advena).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nuphar.
OX   NCBI_TaxID=77108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15944438; DOI=10.1093/molbev/msi191;
RA   Leebens-Mack J., Raubeson L.A., Cui L., Kuehl J.V., Fourcade M.H.,
RA   Chumley T.W., Boore J.L., Jansen R.K., dePamphilis C.W.;
RT   "Identifying the basal angiosperm node in chloroplast genome phylogenies:
RT   sampling one's way out of the Felsenstein zone.";
RL   Mol. Biol. Evol. 22:1948-1963(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17573971; DOI=10.1186/1471-2164-8-174;
RA   Raubeson L.A., Peery R., Chumley T.W., Dziubek C., Fourcade H.M.,
RA   Boore J.L., Jansen R.K.;
RT   "Comparative chloroplast genomics: analyses including new sequences from
RT   the angiosperms Nuphar advena and Ranunculus macranthus.";
RL   BMC Genomics 8:174-174(2007).
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   -!- COFACTOR:
CC       Note=Binds multiple chlorophylls. PSII binds additional chlorophylls,
CC       carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01495};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC       evolving complex and a large number of cofactors. It forms dimeric
CC       complexes. {ECO:0000255|HAMAP-Rule:MF_01495}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01495}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01495}.
CC   -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01495}.
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DR   EMBL; DQ069651; AAZ04083.1; -; Genomic_DNA.
DR   EMBL; DQ354691; ABC60484.1; -; Genomic_DNA.
DR   RefSeq; YP_001001560.1; NC_008788.1.
DR   AlphaFoldDB; Q4FFN0; -.
DR   SMR; Q4FFN0; -.
DR   GeneID; 4699665; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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   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   3: Inferred from homology;
KW   Chlorophyll; Chloroplast; Chromophore; Membrane; Photosynthesis;
KW   Photosystem II; Plastid; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..508
FT                   /note="Photosystem II CP47 reaction center protein"
FT                   /id="PRO_0000359845"
FT   TRANSMEM        21..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        101..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        140..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        203..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        237..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        457..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
SQ   SEQUENCE   508 AA;  56171 MW;  689334B293BB6A65 CRC64;
     MGLPWYRVHT VVLNDPGRLL SVHIMHTALV SGWAGSMALY ELAVFDPSDP VLDPMWRQGM
     FVIPFMTRLG ITNSWGGWSI TGGTITNPGI WSYEGVAGAH IVFSGLCFLA AIWHWVYWDL
     EIFCDERTGK PSLDLPKIFG IHLFLSGVAC FGFGAFHVTG LYGPGIWVSD PYGLTGKVQP
     ISPSWGAEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKALR MGNIETVLSS
     SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVNA GLAENLSLSE
     SWSKIPDKLA FYDYIGNNPA KGGLFRAGSM DNGDGIAVGW LGHPIFRDKE GHELFVRRMP
     TFFETFPVVL VDGDGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELDGVS YNDPATVKKY
     ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHASFAL LFFFGHIWHG ARTLFRDVFA
     GIDPDLDAQV EFGTFQKLGD PTTRRQVV
 
 
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