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