LCL3_ASPCL
ID LCL3_ASPCL Reviewed; 291 AA.
AC A1CRW4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=ACLA_031180;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW08385.1; -; Genomic_DNA.
DR RefSeq; XP_001269811.1; XM_001269810.1.
DR AlphaFoldDB; A1CRW4; -.
DR STRING; 5057.CADACLAP00001915; -.
DR EnsemblFungi; EAW08385; EAW08385; ACLA_031180.
DR GeneID; 4700592; -.
DR KEGG; act:ACLA_031180; -.
DR VEuPathDB; FungiDB:ACLA_031180; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000006701; 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..291
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408642"
FT TRANSMEM 53..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 91..259
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 291 AA; 34044 MW; 67B70C1EB8DC9701 CRC64;
MRWPPWASES QAQQHNTKPP IEHNEKEHGS KSKSWESSVT AIDWAAFAEP RTIIPTVILT
SGFLGAFHIH RRYLRRFPDA GSITPSHFRR RSLLGRVTSV GDGDNFRLYH TPGGRLAGWG
WLPWKKVPTS KKELRDKTVH IRLAGVDAPE LAHFGRPEQP FAREAHQWLT SYLLNRRVRA
YIHRPDQYQR AVATVYVRRA LDFPIPFRRR DVSYEMLKQG LATVYEAKWG AEFGGEAMER
KYRKAEWWAK LRGTGLWKDF RRNEKEWESP RAYKTRMGLE EAVQPRVESK K