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LCL3_COCP7
ID   LCL3_COCP7              Reviewed;         311 AA.
AC   C5P0Z4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable endonuclease LCL3;
DE            EC=3.1.-.-;
GN   Name=LCL3; ORFNames=CPC735_070340;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; ACFW01000009; EER29352.1; -; Genomic_DNA.
DR   RefSeq; XP_003071497.1; XM_003071451.1.
DR   AlphaFoldDB; C5P0Z4; -.
DR   SMR; C5P0Z4; -.
DR   EnsemblFungi; EER29352; EER29352; CPC735_070340.
DR   GeneID; 9696991; -.
DR   KEGG; cpw:CPC735_070340; -.
DR   VEuPathDB; FungiDB:CPC735_070340; -.
DR   HOGENOM; CLU_046484_0_1_1; -.
DR   Proteomes; UP000009084; 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..311
FT                   /note="Probable endonuclease LCL3"
FT                   /id="PRO_0000408656"
FT   TRANSMEM        76..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..275
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ   SEQUENCE   311 AA;  35309 MW;  F4BAA6A296BA2A58 CRC64;
     MKWLFWASPP QDDSNSNSGA ASQVKCRNNE NVDVPAPSNA APPSDRTISK VQSSSRDWNS
     IVNATDWKQF TEPRTIIPTA LVTGGILLCV HIHRKYLRRI PEAGHISPSF FRRRSLLGKV
     TSVGDGDNFR MYHTPGGKLG GWEWWRKVPT GKNELKNRTI HVRLAGVDAP ELPHFGRPAQ
     PFSQEAHSWL TNYILGRRVR AHLYRPDQYG RVVATVYVRR WLFFRQDVGL QMLKHGLATV
     YEAKTGVEFG GVELERQYRE AEACAKKKGK GMWKALKGGT KGEWESPREY KTRMAAEEGQ
     KKNARGITRK K
 
 
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