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BCP_PEA
ID   BCP_PEA                 Reviewed;         189 AA.
AC   Q41001;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Blue copper protein;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Line 59; TISSUE=Pod;
RA   Drew J.E.;
RL   Thesis (1994), Durham University, United Kingdom.
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DR   EMBL; Z25471; CAA80963.1; -; mRNA.
DR   PIR; T06555; T06555.
DR   AlphaFoldDB; Q41001; -.
DR   SMR; Q41001; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR039391; Phytocyanin.
DR   InterPro; IPR003245; Phytocyanin_dom.
DR   PANTHER; PTHR33021; PTHR33021; 1.
DR   Pfam; PF02298; Cu_bind_like; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
DR   PROSITE; PS51485; PHYTOCYANIN; 1.
PE   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Electron transport; Glycoprotein; Metal-binding;
KW   Signal; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..189
FT                   /note="Blue copper protein"
FT                   /id="PRO_0000002870"
FT   DOMAIN          25..124
FT                   /note="Phytocyanin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   REGION          127..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         106
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         111
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        78..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
SQ   SEQUENCE   189 AA;  19319 MW;  8B6EB652C7145098 CRC64;
     MAFSNALVLC FLLAIINMAL PSLATVYTVG DTSGWVIGGD YSTWASDKTF AVGDSLVFNY
     GAGAHTVDEV KESDYKSCTS GNSISTDSTG ATTIPLKKAG KHYFICGVPG HSTGGMKLSI
     KVKASSGSSA APSATPSSSG KGSPSSDDTP AATTTTTTPT KQNESSATSL SPIVALFFTV
     SWICSYVLV
 
 
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