ID B8NNH5_ASPFN Unreviewed; 234 AA.
AC B8NNH5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=60S acidic ribosomal protein P1 {ECO:0000313|EMBL:EED48563.1};
GN ORFNames=AFLA_127860 {ECO:0000313|EMBL:EED48563.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED48563.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED48563.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00011266}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000256|ARBA:ARBA00005436}.
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DR EMBL; EQ963481; EED48563.1; -; Genomic_DNA.
DR RefSeq; XP_002381979.1; XM_002381938.1.
DR AlphaFoldDB; B8NNH5; -.
DR STRING; 332952.B8NNH5; -.
DR EnsemblFungi; EED48563; EED48563; AFLA_127860.
DR VEuPathDB; FungiDB:AFLA_012600; -.
DR eggNOG; KOG1762; Eukaryota.
DR HOGENOM; CLU_1184784_0_0_1; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR CDD; cd05831; Ribosomal_P1; 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_P1/P2.
DR PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR PANTHER; PTHR45696:SF10; 60S ACIDIC RIBOSOMAL PROTEIN P1-RELATED; 1.
DR Pfam; PF00428; Ribosomal_60s; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000313|EMBL:EED48563.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 24904 MW; 106C51EFA2493EF2 CRC64;
MSTAELACSY AALILADDGI EVTADKLQTL LTAAKVQEVE PIWTSIFAKA LEGKDIKDLL
TNVGSGGAAP AGAAAAAGGA AAPAEAAAEE KKEEGNDSIH EESAKVCGVL TFAHREGGVR
RGHGLRSFRL SVFTRSAFLI SFFTSFLPYL LFALAFLVPH TTRPHDDQKG KFKRDQRTKT
SGGTGRFACM MGSMTGTGTD DAMIPAIRLQ SWHTYGSGAR SCWPSSFLCY MFPV
//