LCL3_PARBD
ID LCL3_PARBD Reviewed; 348 AA.
AC C1GKM1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=PADG_07807;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
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; KN275968; EEH42987.1; -; Genomic_DNA.
DR RefSeq; XP_010763158.1; XM_010764856.1.
DR AlphaFoldDB; C1GKM1; -.
DR SMR; C1GKM1; -.
DR STRING; 121759.XP_010763158.1; -.
DR EnsemblFungi; EEH42987; EEH42987; PADG_07807.
DR GeneID; 22586231; -.
DR KEGG; pbn:PADG_07807; -.
DR VEuPathDB; FungiDB:PADG_07807; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR Proteomes; UP000001628; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..348
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408671"
FT TRANSMEM 99..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 137..302
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 348 AA; 39390 MW; 7BB40823A30634AD CRC64;
MRWLFWSSGS QQAPNNNKDN NNNNNNNNDD DDDNNNIIII NNNINRRPPL TLECPSPSHP
PCASCSTKAT TFPSNPKRGW NTSLTARDWA GEFKDPRNLI PTLLLTGGIL FCVRIHRQYL
RRIPLATNIS PTYFHKRSLF GRVTSVGDGD NFRMYHTPGG RLAGWEWLPF RRVPRVKKEL
KDRTIHIRLA GIDAPELPHF GRPAQPYSHA AHTWLTNYLL NKRVRAFPYR QDQYGRVVAT
VYVRRFPWIF LRRDVGLQML RAGMATVYEA KSGVEFGGEG KESKYRRAEE MAKRRGRGLW
KGWKGAGWES PREYKNRMAG VEGERAAAAA AAAGVGGMGE LGVNGGKN
