RL44E_DESA1
ID RL44E_DESA1 Reviewed; 103 AA.
AC B8D537;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=50S ribosomal protein L44e {ECO:0000255|HAMAP-Rule:MF_01476};
GN Name=rpl44e {ECO:0000255|HAMAP-Rule:MF_01476}; OrderedLocusNames=DKAM_0892;
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n;
RX PubMed=19114480; DOI=10.1128/jb.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01476}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01476};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01476};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01476}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.
CC {ECO:0000255|HAMAP-Rule:MF_01476}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACL11218.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; CP001140; ACL11218.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B8D537; -.
DR SMR; B8D537; -.
DR STRING; 490899.DKAM_0892; -.
DR EnsemblBacteria; ACL11218; ACL11218; DKAM_0892.
DR KEGG; dka:DKAM_0892; -.
DR eggNOG; arCOG04109; Archaea.
DR HOGENOM; CLU_114645_3_0_2; -.
DR Proteomes; UP000006903; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01476; Ribosomal_L44e; 1.
DR InterPro; IPR000552; Ribosomal_L44e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR10369; PTHR10369; 1.
DR Pfam; PF00935; Ribosomal_L44; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01172; RIBOSOMAL_L44E; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..103
FT /note="50S ribosomal protein L44e"
FT /id="PRO_0000419125"
FT ZN_FING 18..81
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01476"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01476"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01476"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01476"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01476"
SQ SEQUENCE 103 AA; 12055 MW; D231B52B34C1198C CRC64;
MCLRVLDLRI PKVIITYCPK CRTHTEHSVT IYKHGKRRSL SEGERRYARK KKGYGSKRKP
EQKRFAKVTK KTVLKLKCSK CGYIIHREGI RLKKAELVEV GGR
