LCL3_PARBP
ID LCL3_PARBP Reviewed; 342 AA.
AC C0SEQ8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=PABG_06163;
OS Paracoccidioides brasiliensis (strain Pb03).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=482561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb03;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LCL3 family. {ECO:0000305}.
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DR EMBL; KN305541; EEH16076.1; -; Genomic_DNA.
DR AlphaFoldDB; C0SEQ8; -.
DR SMR; C0SEQ8; -.
DR EnsemblFungi; EEH16076; EEH16076; PABG_06163.
DR VEuPathDB; FungiDB:PABG_06163; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; C0SEQ8; -.
DR Proteomes; UP000002740; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 3: Inferred from homology;
KW Calcium; Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Nuclease; Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408672"
FT TRANSMEM 93..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 131..296
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 342 AA; 38491 MW; 992AE6F284A73EB4 CRC64;
MRWLFWSSGS QQAPNSNKDN NNNNDGDDDN NNIIINNINR RPPLTLECPS PSHPPCASCS
TKATTSPSNP KRGWNTSLTA RDWAGEFKDP RNLIPTLLLT GGILFCVRIH RQYLRRIPLA
TNISPTYFHK RSLFGRVTSV GDGDNFRMYH TPGGRLAGWE WLPFRRVPRV KKELKDRTIH
IRLAGIDAPE LPHFGRPAQP YSHAAHTWLT NYLLNKRVRA FPYRQDQYGR VVATVYVRRF
PWIFLRRDVG LQMLRAGMAT VYEAKSGVEF GGEGKESKYR RAEEMAKRRG RGLWKGWKGA
GWESPREYKN RMAGVEGERA AAGGGGGGVG GMGELGVNGG KN