RL5_ANOGA
ID RL5_ANOGA Reviewed; 325 AA.
AC O44248; Q5TNI8; Q7PWA8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=60S ribosomal protein L5;
GN Name=RpL5; ORFNames=AGAP009031;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=G3;
RA Cornel A.J., Kumar V., Mukabayire O., Salazar Rafferty C., Petrarca V.,
RA Coluzzi M., Collins F.H.;
RT "A comprehensive physical map of the malaria vector Anopheles gambiae.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000250|UniProtKB:P26321}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU).
CC {ECO:0000250|UniProtKB:P26321}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26321}. Nucleus
CC {ECO:0000250|UniProtKB:P26321}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA14773.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF002238; AAB97731.1; -; mRNA.
DR EMBL; AAAB01008984; EAA14773.3; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_319782.3; XM_319782.5.
DR AlphaFoldDB; O44248; -.
DR SMR; O44248; -.
DR STRING; 7165.AGAP009031-PA; -.
DR GeneID; 1279989; -.
DR KEGG; aga:AgaP_AGAP009031; -.
DR CTD; 1279989; -.
DR VEuPathDB; VectorBase:AGAP009031; -.
DR eggNOG; KOG0875; Eukaryota.
DR HOGENOM; CLU_056222_1_0_1; -.
DR InParanoid; O44248; -.
DR OrthoDB; 999609at2759; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR InterPro; IPR025607; Rbsml_L5e_C.
DR PANTHER; PTHR23410; PTHR23410; 1.
DR Pfam; PF14204; Ribosomal_L18_c; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..325
FT /note="60S ribosomal protein L5"
FT /id="PRO_0000131441"
FT REGION 247..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 67
FT /note="A -> R (in Ref. 1; AAB97731)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> S (in Ref. 1; AAB97731)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="R -> RK (in Ref. 1; AAB97731)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> RL (in Ref. 1; AAB97731)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="RR -> QG (in Ref. 1; AAB97731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 37782 MW; 9C04C249A89B3C42 CRC64;
MGFVKVVKNK QYFKRYQVRF RRRREGKTDY YARKRLIFQD KNKYNTPKFR LIVRLSNRDI
TCQIAYARIE GDRIVCAAYS HELPRYGVKV GLTNYAAAYC TGLLVARRIL QKLRLDTLYA
GCTDVTGEEY LVEPVDEGPA AFRCYLDVGL ARTTTGARVF GAMKGAVDGG LNIPHSVKRF
PGYSAENKSF NAEMHRDHIF GLHVANYMRT LEEEDEEAFK RQFSKYISLG IKADDIENIY
KNAHASIRIP PSRRNPRRRS PRSGGRWPSC RSPPARRRSR STRPTSWPRS RPTSKPKRPR
RRRPFFFSSW WCIILVLPCS SPVRR
