LCL3_TALMQ
ID LCL3_TALMQ Reviewed; 344 AA.
AC B6QNP4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=PMAA_053390;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995903; EEA21532.1; -; Genomic_DNA.
DR RefSeq; XP_002150141.1; XM_002150105.1.
DR AlphaFoldDB; B6QNP4; -.
DR SMR; B6QNP4; -.
DR STRING; 441960.B6QNP4; -.
DR EnsemblFungi; EEA21532; EEA21532; PMAA_053390.
DR GeneID; 7027666; -.
DR KEGG; tmf:PMAA_053390; -.
DR VEuPathDB; FungiDB:PMAA_053390; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OrthoDB; 1333771at2759; -.
DR PhylomeDB; B6QNP4; -.
DR Proteomes; UP000001294; 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..344
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408674"
FT TRANSMEM 77..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 115..282
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 344 AA; 39258 MW; B60B6C6FD10EEB64 CRC64;
MGWWSLGSSG SKADPEKSKA NDSKSSNRRQ QEEGEQSFIP PPLTSRTSSS SSSKSTTDWN
SSLNAFDWSQ FKQPRNLIPT ALLTGGILFV VYVQRRYLRR FPEATDISSS YFRSRSLLGR
VTSVGDGDNF RIFHTPGGRL VGWGWLPWMK VPTARKELKD KTVHIRLAGV DAPELAHFGR
PAQPYAYEAH MWLTSYLMNR RVRAYVHRPD QYKRVIATVY VRRWLDFPPL RRRDVSYEML
RRGLATVYEA KSGVEFGGTE NERKYREAEM LAKNRRQGLW KDFGKRGGVN FESPREYKTR
MQSLDMSAES SSSSSSSSNT EKNPGLVGSL LRKVWPFGSK KDGT