ID E9B5B9_LEIMU Unreviewed; 213 AA.
AC E9B5B9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=rRNA maturation factor {ECO:0008006|Google:ProtNLM};
GN ORFNames=LMXM_33_3300 {ECO:0000313|EMBL:CBZ30439.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ30439.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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DR EMBL; FR799586; CBZ30439.1; -; Genomic_DNA.
DR RefSeq; XP_003878886.1; XM_003878837.1.
DR AlphaFoldDB; E9B5B9; -.
DR GeneID; 13452494; -.
DR KEGG; lmi:LMXM_33_3300; -.
DR VEuPathDB; TriTrypDB:LmxM.33.3300; -.
DR OMA; VELSIHF; -.
DR OrthoDB; 168887at2759; -.
DR PhylomeDB; E9B5B9; -.
DR Proteomes; UP000007259; Chromosome 33.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR Gene3D; 3.40.390.30; Metalloproteases ('zincins'), catalytic domain; 1.
DR HAMAP; MF_00009; Endoribonucl_YbeY; 1.
DR InterPro; IPR023091; MetalPrtase_cat_dom_sf_prd.
DR InterPro; IPR002036; YbeY.
DR InterPro; IPR020549; YbeY_CS.
DR Pfam; PF02130; YbeY; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS01306; UPF0054; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 213 AA; 23985 MW; 92D3CE2EBDF6A4B0 CRC64;
MKTFKHLTIT GATPTLRRET RYLMHLLLTL ERAPYDTRLN LEFVSLAHMR QLNYKYKGSD
RATDVLTFTP VGKAGSFVND LLFSDFLERG DGNKDTGATL TTSPTCAGAV GAEPNALTQS
IIRAELLDLG NIFVSLDYMR LRCRRYPSTT LPLAPYLHAA LVHATLHALG YDHTSPALLQ
QMVRREQQLG RQLAMIARQH PRCLPPLNMW DTM
//