LCL3_ASPNC
ID LCL3_ASPNC Reviewed; 275 AA.
AC A2Q8K8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=An01g04700;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM269963; CAK37005.1; -; Genomic_DNA.
DR RefSeq; XP_001388897.1; XM_001388860.1.
DR AlphaFoldDB; A2Q8K8; -.
DR SMR; A2Q8K8; -.
DR PaxDb; A2Q8K8; -.
DR PRIDE; A2Q8K8; -.
DR EnsemblFungi; CAK37005; CAK37005; An01g04700.
DR GeneID; 4977593; -.
DR KEGG; ang:ANI_1_2496014; -.
DR VEuPathDB; FungiDB:An01g04700; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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..275
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408646"
FT TRANSMEM 41..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 79..247
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 275 AA; 31814 MW; 468365248EAA3C5D CRC64;
MRWPPWASNT QASNNDHPTT TNNNDPKNLL DWSAFTELRT LIPTLVLTTG ILSAFTLHRN
YLRRFPTAVN ITPAYYRRRS ILGKVTSVGD GDNFRIYHTP GGRLAGWGWV PWKKVPTTRK
ELRDQTIHVR IAGVDAPEQA HFGRPAQPFG KEAHEWLTGY LINRRVRIYV HRQDQYQRVV
ATVFVRRALD FPVPFRRRDV GYEMLRKGLA TVYEAKVGAE FGGEVMEKKY RSAEWWAKAR
GLGLWKGFKK NRDAWESPRE FKTRTGMEDV GDGKK