ID E9B109_LEIMU Unreviewed; 545 AA.
AC E9B109;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Conserved zinc-finger protein {ECO:0000313|EMBL:CBZ28914.1};
GN ORFNames=LMXM_29_2360 {ECO:0000313|EMBL:CBZ28914.1};
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:CBZ28914.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|EMBL:CBZ28914.1, ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ28914.1,
RC 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; FR799582; CBZ28914.1; -; Genomic_DNA.
DR RefSeq; XP_003877380.1; XM_003877331.1.
DR AlphaFoldDB; E9B109; -.
DR GeneID; 13451483; -.
DR KEGG; lmi:LMXM_29_2360; -.
DR VEuPathDB; TriTrypDB:LmxM.29.2360; -.
DR OMA; CGICFNV; -.
DR OrthoDB; 4323694at2759; -.
DR PhylomeDB; E9B109; -.
DR Proteomes; UP000007259; Chromosome 29.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19757; Bbox1; 1.
DR CDD; cd19756; Bbox2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047153; TRIM45/56/19.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462:SF302; B BOX-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 8..49
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 138..177
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT COILED 185..212
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 545 AA; 60831 MW; F1B35231A4423774 CRC64;
MPARVITCGI CFNVLDHPLT FDCHHSFCTG CVRRLLSENA NNGFQCPLCA TSYTEVHSHN
LAQYADHEAE VYVEVLALGT SNSPKCQWCE TTSAKVQCGE CMCVYCEDCC IAVHKNSAKR
DHAIGKLSES SRNFIPRCPL RGHEEYRAEF FCSQCRQVCC AYCLQVGPHR DHLHMTVAVA
AAEARQQLSR DMESLLEVKH RLEQQAAEMN RVSVLYSDTY DAVENIVTER FEAFKQQLMQ
RELEVRRTLT NLRDSGDAAL TTSRRQYLDK LNSVNETLLQ FRTIHNGGTD DEVLKRHSQF
GKCLNTDLPA VTGSGFKVVS LGEMTLTSLD IGLDLQTIEH NQPIFPRLNR SVRHSTASNL
SMNGGSVSPF AGNTLSTPLR LTFPVDDDVE ATVLAEGVRL RCVASGGRDT QIGVRSKEMF
QTLLGQFPED RSVVSWQVRL DSISDTFIGV VEKTSQASEV PEGFYWKAAC ADVIDGRIGR
YTAAVRRLPV CRNGDRIRFL YDGVQGTLRI VVNDSDDRGV VVSDLHPRIA ACFIFYPGES
LTILF
//