ID D2VJC9_NAEGR Unreviewed; 616 AA.
AC D2VJC9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=S5 DRBM domain-containing protein {ECO:0000259|PROSITE:PS50881};
GN ORFNames=NAEGRDRAFT_80176 {ECO:0000313|EMBL:EFC43017.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC43017.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC43017.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000256|ARBA:ARBA00008945, ECO:0000256|RuleBase:RU003823}.
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DR EMBL; GG738876; EFC43017.1; -; Genomic_DNA.
DR RefSeq; XP_002675761.1; XM_002675715.1.
DR AlphaFoldDB; D2VJC9; -.
DR STRING; 5762.D2VJC9; -.
DR EnsemblProtists; EFC43017; EFC43017; NAEGRDRAFT_80176.
DR GeneID; 8852070; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_80176; -.
DR eggNOG; KOG0877; Eukaryota.
DR InParanoid; D2VJC9; -.
DR OrthoDB; 5479674at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000851; Ribosomal_uS5.
DR InterPro; IPR005324; Ribosomal_uS5_C.
DR InterPro; IPR013810; Ribosomal_uS5_N.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|PROSITE-
KW ProRule:PRU00268};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|PROSITE-
KW ProRule:PRU00268}.
FT DOMAIN 443..506
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
FT REGION 216..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 70821 MW; BAA1EFEC9D1DEA1F CRC64;
MRNIKLLRQL PSSTKKLATK QSPLCFSSIH NSPSYIQSRC FSSSKIIKNS FERISDSELK
QMEEKERNRE IPAEELNFPT TDNDKDFINI IEAKQQGTKF TEEMFETLVF YLKNLRKEKR
HKVVYWLATE KKETKLVRKI KEAFISLSLL QANVNLQLPR AVQKERIWAK YTNFGMFPGT
FSQPAETEYN RFKVKSLYDL SKLKTQADLD DLDEMVDEDN ISRRDQDEDN ENEQMEEIED
EEEVGSNEID TIDIEDVDEN IPINELQEAL RVRKDYSRFH ELIEEKNEAD PERIQVPKSF
ERVSQDVENL GKLQGKRFKV SKVDQSDMIK SLNTKLLRQE RDETSAPFYL YQFDETQLGQ
QIQNLESIIE GKSSKTNVSV NPIYNASVGV EKGYFGDVDL DADWDESLYE YEGEPAITHP
LADDVEDPEI YHGQKDAITD VSFEEKVLKL SRNCKMTTGG RVESYNCLYL VGSYSGLCGV
GFGTAASPAV AQSKARKAAY KNIRSIDPSA CIPRSHMLEA KFGACKVRIH PSTKEQPTAN
PILRKLCAYL GLKYCSVRLY GSRNILNVIP AFFKCVDQLR SVDRDAAMRG VMPIYLKKDF
EDYLEKVRVG KGLYGW
//