RLA2_ASPFU
ID RLA2_ASPFU Reviewed; 111 AA.
AC Q9UUZ6; Q4X1G0; Q9HGU9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=60S acidic ribosomal protein P2;
DE AltName: Full=AfP2;
DE AltName: Allergen=Asp f 8;
GN ORFNames=AFUA_2G10100;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42202 / AF-102 / Ag 507;
RA Hemmann S., Crameri R.;
RT "Highly conserved ribosomal proteins binding to serum IgE of Aspergillus
RT fumigatus sensitized individuals.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11849550; DOI=10.1046/j.1365-2958.2002.02736.x;
RA Santos C., Ballesta J.P.G.;
RT "Role of the ribosomal stalk components in the resistance of Aspergillus
RT fumigatus to the sordarin antifungals.";
RL Mol. Microbiol. 43:227-237(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ224333; CAB64688.1; -; mRNA.
DR EMBL; AF268870; AAG01801.1; -; Genomic_DNA.
DR EMBL; AAHF01000001; EAL93305.1; -; Genomic_DNA.
DR RefSeq; XP_755343.1; XM_750250.1.
DR AlphaFoldDB; Q9UUZ6; -.
DR SMR; Q9UUZ6; -.
DR STRING; 746128.CADAFUBP00002532; -.
DR Allergome; 3126; Asp f 8.0101.
DR Allergome; 78; Asp f 8.
DR EnsemblFungi; EAL93305; EAL93305; AFUA_2G10100.
DR GeneID; 3512932; -.
DR KEGG; afm:AFUA_2G10100; -.
DR VEuPathDB; FungiDB:Afu2g10100; -.
DR eggNOG; KOG3449; Eukaryota.
DR HOGENOM; CLU_114656_0_2_1; -.
DR InParanoid; Q9UUZ6; -.
DR OMA; AYLMNVL; -.
DR OrthoDB; 1626327at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR CDD; cd05833; Ribosomal_P2; 1.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_L12/P1/P2.
DR InterPro; IPR044076; Ribosomal_P2.
DR InterPro; IPR001859; T.cruzi_P2-like.
DR PANTHER; PTHR21141; PTHR21141; 1.
DR PRINTS; PR00456; RIBOSOMALP2.
PE 1: Evidence at protein level;
KW Allergen; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..111
FT /note="60S acidic ribosomal protein P2"
FT /id="PRO_0000157673"
FT REGION 81..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="H -> Y (in Ref. 1; CAB64688)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="Y -> F (in Ref. 1; CAB64688)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="E -> K (in Ref. 1; CAB64688)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="K -> N (in Ref. 1; CAB64688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 11141 MW; 0B4C19B5CEE25471 CRC64;
MKHLAAYLLL ALAGNTSPSS EDVKAVLSSV GIDADEERLN KLIAELEGKD LQELIAEGST
KLASVPSGGA AAAAPAAAGA AAGGAAAPAA EEKKEEEKEE SDEDMGFGLF D