RL36_EMENI
ID RL36_EMENI Reviewed; 105 AA.
AC P9WEU2; A0A1U8QU64; C8V8I8; Q5B4S8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=60S ribosomal protein L36 {ECO:0000305};
GN ORFNames=AN4452-2, ANIA_04452-2;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules (By similarity). The large subunit (LSU) contains the
CC ribosomal catalytic site termed the peptidyl transferase center (PTC),
CC which catalyzes the formation of peptide bonds, thereby polymerizing
CC the amino acids delivered by tRNAs into a polypeptide chain (By
CC similarity). The nascent polypeptides leave the ribosome through a
CC tunnel in the LSU and interact with protein factors that function in
CC enzymatic processing, targeting, and the membrane insertion of nascent
CC chains at the exit of the ribosomal tunnel (By similarity).
CC {ECO:0000250|UniProtKB:O14455}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU).
CC {ECO:0000250|UniProtKB:O14455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14455}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL36 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF77490.1; Type=Erroneous gene model prediction; Note=The predicted gene ANIA_04452 has been split into 2 genes: ANIA_04452-1 and ANIA_04452-2.; Evidence={ECO:0000305};
CC Sequence=EAA60217.1; Type=Erroneous gene model prediction; Note=The predicted gene ANIA_04452 has been split into 2 genes: ANIA_04452-1 and ANIA_04452-2.; Evidence={ECO:0000305};
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DR EMBL; AACD01000077; EAA60217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001303; CBF77490.1; ALT_SEQ; Genomic_DNA.
DR SMR; P9WEU2; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.10.10.1760; -; 1.
DR InterPro; IPR038097; L36e_sf.
DR InterPro; IPR000509; Ribosomal_L36e.
DR Pfam; PF01158; Ribosomal_L36e; 1.
DR PROSITE; PS01190; RIBOSOMAL_L36E; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..105
FT /note="60S ribosomal protein L36"
FT /id="PRO_0000453677"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 105 AA; 11888 MW; 1EAE24CDDAAFEFCE CRC64;
MAQERSGIAV GLNKGHKTTP LNTPKTRISR SKGKASRRTA FVRDIAREVV GLAPYERRVI
ELLRNAQDKR ARKLAKKRLG TFTRGKRKVE DMQRVIAEAR RVGAH
