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Database: UniProt
Entry: A7A295_YEAS7
LinkDB: A7A295_YEAS7
Original site: A7A295_YEAS7 
ID   A7A295_YEAS7            Unreviewed;       338 AA.
AC   A7A295;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   13-JUN-2012, entry version 24.
DE   SubName: Full=Conserved protein;
DE   Flags: Fragment;
GN   OrderedLocusNames=SCY_4014;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R.,
RA   Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
RA   Li Y., Davis R.W., Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces
RT   cerevisiae strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Capsid protein (CA) is the structural component of the
CC       virus-like particle (VLP), forming the shell that encapsulates the
CC       retrotransposons dimeric RNA genome. The particles are assembled
CC       from trimer-clustered units and there are holes in the capsid
CC       shells that allow for the diffusion of macromolecules. CA has also
CC       nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met
CC       annealing to the multipartite primer-binding site (PBS),
CC       dimerization of Ty1 RNA and initiation of reverse transcription
CC       (By similarity).
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; AAFW02000182; EDN59098.1; -; Genomic_DNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR015820; Retrotransposon_Ty1A_N.
DR   Pfam; PF01021; TYA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm.
FT   NON_TER     338    338
SQ   SEQUENCE   338 AA;  37565 MW;  4B3478C49B02CD55 CRC64;
     MESQQLSQHS PISHGSACAS VTSKEVQTTQ DPLDISASKT EECEKVSTQA NSQQPTTPPS
     SAVPENHHHA SPQAAQVPLP QNGPYPQQRM MNTQQANISG WPVYGHPSLM PYPPYQMSPM
     YAPPGAQSQF TQYPQYVGTH LNTPSPESGN SFPDSSSAKS NMTSTNQHVR PPPILTSPND
     FLNWVKIYIK FLQNSNLGDI IPTATRKAVR QMTDDELTFL CHTFQLFAPS QFLPPWVKDI
     LSVDYTDIMK ILSKSINKMQ SDTQEVNDIT TLATLHYNGS TPADAFEAEV TNILDRLNNN
     GIPINNKVAC QFIMRGLSGE YKFLRYARHR CIHMTVAD
//
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