LCL3_PARBA
ID LCL3_PARBA Reviewed; 348 AA.
AC C1H492;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=PAAG_05585;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
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; KN294006; EEH34536.1; -; Genomic_DNA.
DR RefSeq; XP_002792300.1; XM_002792254.1.
DR AlphaFoldDB; C1H492; -.
DR SMR; C1H492; -.
DR STRING; 502779.C1H492; -.
DR EnsemblFungi; EEH34536; EEH34536; PAAG_05585.
DR GeneID; 9095599; -.
DR KEGG; pbl:PAAG_05585; -.
DR VEuPathDB; FungiDB:PAAG_05585; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000002059; Partially assembled 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_0000408670"
FT TRANSMEM 91..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 129..294
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 348 AA; 39108 MW; FD26E43A9F02BB66 CRC64;
MRWLFWSSGS QQAPNNKDNN NSNNNDDDDD DYDNNINKRP PLTPESPSPS HPPCASCSTQ
ATASFSNPRR DWNTSLTAHD WAGEFKDPRN LIPTLLLTGG ILFCVRIHRQ YLRRIPLATN
ISPTYFHKRS LFGRVTSVGD GDNFRMYHTP GGRLAGWEWL PFRRVPRVKK ELKDRTIHIR
LAGIDAPELP HFGRPAQPYS HAAHTWLTNY LLNKRVRVFP YRQDQYGRVV ATVYVRRFPW
IFLRRDVGLQ MLRAGMATVY EAKSGVEFGG EGKESKYRRA EEVAKRRGRG LWKGWKGVGW
ESPREYKNRM AGVEGEKAAA AAAAAAAAAA AAAGVGGMGE LGVNGEKN