LOCUS YP_009266430 477 aa linear PLN 03-APR-2023
DEFINITION ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit
(chloroplast) [Oryza brachyantha].
ACCESSION YP_009266430
VERSION YP_009266430.1
DBLINK BioProject: PRJNA927338
DBSOURCE REFSEQ: accession NC_030596.1
KEYWORDS RefSeq.
SOURCE chloroplast Oryza brachyantha (malo sina)
ORGANISM Oryza brachyantha
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP
clade; Oryzoideae; Oryzeae; Oryzinae; Oryza.
REFERENCE 1 (residues 1 to 477)
AUTHORS Liu,F., Tembrock,L.R., Sun,C., Han,G., Guo,C. and Wu,Z.
TITLE The complete plastid genome of the wild rice species Oryza
brachyantha (Poaceae)
JOURNAL Mitochondrial DNA Part B Resour (2016) In press
REFERENCE 2 (residues 1 to 477)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (12-JUL-2016) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 477)
AUTHORS Wu,Z.
TITLE Direct Submission
JOURNAL Submitted (03-NOV-2015) Department of Biology, Colorado State
University, Campus Delivery 1878, Fort Collins, CO 80523, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence is identical to ANJ78518.
COMPLETENESS: full length.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..477
/organism="Oryza brachyantha"
/organelle="plastid:chloroplast"
/db_xref="taxon:4533"
Protein 1..477
/product="ribulose 1,5-bisphosphate carboxylase/oxygenase
large subunit"
/calculated_mol_wt=52793
Region 1..475
/region_name="rbcL"
/note="ribulose-1,5-bisphosphate carboxylase/oxygenase
large subunit; CHL00040"
/db_xref="CDD:176981"
Site order(45,60,62..63,65..72,75,80,106..110,112,114..115,
118..119,121..123,125..128,130..132,175..179,204..205,
207..211,213,243..248,253,268,271,273..276,278..279,294,
296..297,299..301,303..304,307..309,331..336,381..383,
404..405,407..410,412..413,462,465,467,469..470,472)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:173977"
Site order(60,65..66,123,173,175,177,203..204,294..295,327,
334..335,379..381,403..404)
/site_type="active"
/db_xref="CDD:173977"
Site order(156,161,163..167,194..196,226,229..235,258,263,289,
397,410..411,415,418,421..422,425..426,429,431..433,451,
453)
/site_type="other"
/note="heterodimer interface [polypeptide binding]"
/db_xref="CDD:173977"
Site 201
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:173977"
Site 203..204
/site_type="metal-binding"
/note="metal binding site [ion binding]"
/db_xref="CDD:173977"
CDS 1..477
/gene="rbcL"
/locus_tag="BBW32_gp056"
/coded_by="NC_030596.1:54497..55930"
/transl_table=11
/db_xref="GeneID:33018038"
ORIGIN
1 mspqtetkas vgfqagvkdy kltyytpeye tkdtdilaaf rvtpqpgvpp eeagaavaae
61 sstgtwttvw tdgltsldry kgrcyhiepv vgeenqyiay vaypldlfee gsvtnmftsi
121 vgnvfgfkal ralrledlri pptysktfqg pphgiqverd klnkygrpll gctikpklgl
181 saknygracy eclrggldft kddenvnsqp fmrwrdrfvf caeaiyksqa etgeikghyl
241 natagtceem ikravfarel gvpivmhdyl tggftantsl ahycrdngll lhihramhav
301 idrqknhgmh frvlakalrm sggdhihagt vvgklegere mtlgfvdllr ddfiekdrar
361 gifftqdwvs mpgvipvasg gihvwhmpal teifgddsvl qfgggtlghp wgnapgaaan
421 rvaleacvqa rnegrdlare gneiirsack wspelsaace vwkaikfefe pvdkldn
//