LCL3_ARTGP
ID LCL3_ARTGP Reviewed; 283 AA.
AC E4V094;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=MGYG_06031;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989826; EFR03031.1; -; Genomic_DNA.
DR RefSeq; XP_003171485.1; XM_003171437.1.
DR AlphaFoldDB; E4V094; -.
DR SMR; E4V094; -.
DR STRING; 63402.XP_003171485.1; -.
DR EnsemblFungi; EFR03031; EFR03031; MGYG_06031.
DR GeneID; 10026737; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; E4V094; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000002669; 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..283
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408639"
FT TRANSMEM 57..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 95..256
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 10..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 283 AA; 32206 MW; CC8F329A133C8E7E CRC64;
MRWLFWASDN DKDGCKCNSK SSSSSDEKPT APLKSNKDWN SLSNAINWSH YAEPSNLIPT
VLLTSGILFA FRIHRRYLRR IPEATNISPS YLRQRSILGK VTSVGDGDNF RIYHTPGGML
AGWGWLRKVP TSKKELKNNT IHIRIAGVDA PELAHFGRPS QPFGEEAHKW LINRLTGRRI
RAYVYRPDQY SRIVATVYAY RFLFFPQDIG LQMLREGLAT VYEAKSGAEF GGPEQEKKYR
DAEALAKKKG KGLWKTKGSN DWESPRDFKS RMNAIDQGKD SST