ID   L5LRB2_MYODS            Unreviewed;      1125 AA.
AC   L5LRB2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Large ribosomal subunit protein uL13 {ECO:0000256|ARBA:ARBA00035201};
DE   AltName: Full=60S ribosomal protein L13a {ECO:0000256|ARBA:ARBA00035367};
GN   ORFNames=MDA_GLEAN10005856 {ECO:0000313|EMBL:ELK28587.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK28587.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC       {ECO:0000256|ARBA:ARBA00006227, ECO:0000256|RuleBase:RU003877}.
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; KB109009; ELK28587.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5LRB2; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005125; F:cytokine activity; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00392; Ribosomal_L13; 1.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   Gene3D; 6.10.250.3250; -; 1.
DR   Gene3D; 3.90.1180.10; Ribosomal protein L13; 1.
DR   HAMAP; MF_01366; Ribosomal_L13; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR004213; Flt3_lig.
DR   InterPro; IPR005822; Ribosomal_uL13.
DR   InterPro; IPR023563; Ribosomal_uL13_CS.
DR   InterPro; IPR005755; Ribosomal_uL13_euk/arc.
DR   InterPro; IPR036899; Ribosomal_uL13_sf.
DR   NCBIfam; TIGR01077; L13_A_E; 1.
DR   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 3.
DR   Pfam; PF02947; Flt3_lig; 1.
DR   Pfam; PF00572; Ribosomal_L13; 1.
DR   SUPFAM; SSF47266; 4-helical cytokines; 1.
DR   SUPFAM; SSF53720; ALDH-like; 2.
DR   SUPFAM; SSF52161; Ribosomal protein L13; 1.
DR   PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU003877};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000256|RuleBase:RU003877};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          48..486
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          548..607
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          660..752
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   COILED          1086..1113
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1125 AA;  122120 MW;  E0B464E68AC1DDC5 CRC64;
     MAATRAESRA REIFATLEYG PAPESHACAL AWLDTQDRCL GHYVSGKWLK PGNRKSAPCQ
     DPITGENLAT CLQAQAEDVA AAAEAARAAL ENWSRLPGAS RAKHLTRLAK MIQKHQRLLW
     TLESLVTGRA VREVRDRDVP LAQQLLQYHA IQAHIQEEAL AGWEPMGVIG LILPPTFSFL
     EMMWRICPAL AVGCTVVVLV PSASPTPLLL AQLAGELGHF PGILNVISGP ASLGPVLASQ
     PGVQKVAFCG AIEEGRVLRR TLAGVGPELG LALGTESLLL LTEAADVDSA VEGVVDAAWS
     DRSPGGLRLL VQESVWDEAM RRLQVRMARL RGGRGLDGAG DLGARGAAAR ELAQRYVREA
     QSQGAQVFQA GDVPLDSPFF PPTLVSDLPP SSPCAQAEVP WPLVVASPFR TAKEALAVAN
     GTPRGGSASV WSERLGQALE LGYGLRVGTV WINAHGLRDP AVPMGGCKES GSSWHGGLDG
     LYEYLRPAGT PVRLPYLSEN LNYDTFGLTV PSALPAGPET GPSPAPPYGL FVGGRFQAPG
     ARSSRPIHDS QGNLHGYVAE GGAKDIRVAV EAAHQAAPGW MGQSPGARAA LLLALAAALE
     RREPTLSLRL ERHGVVFLGG PRPGPEPQPA EKEKYHFVVA LIYFWGDRGV AELRGPVLRL
     REPLGVLAVV CPDEWPLLAF VSLLAPALAH GNSVVLVPSE TCPIPALEVC QDMATLLPAG
     LVNVVTGDRD HLTRCLALHQ DVQALWYFGS AQSDYLLQDY PVTVASNLQD DKLCGAFWRL
     VLAQRWMEQL KTVAGSQMEK LLEAVNTEIH FVTLCALQPL PSCLRFVQTN ISHLLQDTSE
     QLVALKPWIT RWNFSGCLEL KCQPDSSTLL PSASPLALAA TALPAPQASL LLLLLLPAAL
     VLLSAACGCL GWGVGKFWMT EPSCLPQVLV LDGRGHLLGR LAAIVAKQVL LGRKVVVVRW
     CGLNISGNFY RNKLKYLAFL RKRMNTNPSR GPYHFRAPSR IFWRTVRGML PHKTKRGQAA
     LDRLKVFDGI PPPYDKKKRM VVPAALKVVR LKPTRKFAYL GRLAHEVGWK YQAVTATLEE
     KRKEKAKMHY RKKKQLMRLR KQAEKNVEKK INKFTEVLKT HGLLV
//