LCL3_ASPFC
ID LCL3_ASPFC Reviewed; 296 AA.
AC B0XMZ5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=AFUB_003840;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP55687.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XMZ5; -.
DR SMR; B0XMZ5; -.
DR EnsemblFungi; EDP55687; EDP55687; AFUB_003840.
DR VEuPathDB; FungiDB:AFUB_003840; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR PhylomeDB; B0XMZ5; -.
DR Proteomes; UP000001699; 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..296
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408643"
FT TRANSMEM 59..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 97..264
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 296 AA; 34461 MW; 57522D4C42E264DA CRC64;
MRWPPWASDT QAQQQSRKSS SEDDERQAAA SSTTTSKKKD WESSVTAIDW AAFTEARTII
PTLILTSGFL GAFYIHRRYL RRFPDAVSIT PSYFRRRSLL GQVTSVGDGD NFRIYHTPGG
RLAGWGWLPW KKIPTSKKEL RDKTVHIRLA GIDAPELAHF GRPEQPFARE AHQWLTSYLF
GRRVRAYIHR PDQYQRAVAS VYVRRLLDFP PFRRRDVSYE MLKRGLATVY EAKIGAEFGG
EAMERKYKKA EWWAKLRGVG LWKDYRRNKT KWESPREYKT RMGLEEAAQP GVEIKK
