LCL3_NEOFI
ID LCL3_NEOFI Reviewed; 295 AA.
AC A1D4S1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=NFIA_021220;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027688; EAW23414.1; -; Genomic_DNA.
DR RefSeq; XP_001265311.1; XM_001265310.1.
DR AlphaFoldDB; A1D4S1; -.
DR SMR; A1D4S1; -.
DR STRING; 36630.CADNFIAP00001239; -.
DR EnsemblFungi; EAW23414; EAW23414; NFIA_021220.
DR GeneID; 4591621; -.
DR KEGG; nfi:NFIA_021220; -.
DR VEuPathDB; FungiDB:NFIA_021220; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000006702; 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..295
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408669"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 96..263
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 295 AA; 34390 MW; 9BB96CDCDC22FEAE CRC64;
MRWPPWASDS QAQQQTAKHD EHDERQAAAK STTTSKKKDW ESSVTAIDWA AFTEARTIIP
TLILTSGFLG AFYIHRRYLR RFPDAVSITP SYFRRRSLLG QVTSVGDGDN FRIYHTPGGR
LAGWGWLPWK KIPTSKKELR DKTVHIRLAG IDAPELAHFG RPEQPFAREA HQWLTSYLLG
RRVRAYIHRP DQYQRAVASV YVRRLLDFPP LRRRDVSYEM LKRGLATVYE AKIGAEFGGE
AMERKYKKAE WWAKLRGVGL WKDYRRNKTK WESPREYKTR MGLEEAAQPP VETKK