ID A0A0D2DSQ2_9EURO Unreviewed; 289 AA.
AC A0A0D2DSQ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404};
DE AltName: Full=Probable endonuclease lcl3 {ECO:0000256|ARBA:ARBA00014651};
GN ORFNames=PV04_07481 {ECO:0000313|EMBL:KIW65202.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW65202.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW65202.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW65202.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the LCL3 family.
CC {ECO:0000256|ARBA:ARBA00005435}.
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DR EMBL; KN846960; KIW65202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2DSQ2; -.
DR STRING; 5601.A0A0D2DSQ2; -.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OrthoDB; 208975at2759; -.
DR Proteomes; UP000054266; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; 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 PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR PANTHER; PTHR12302:SF3; ENDONUCLEASE LCL3-RELATED; 1.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722}.
FT DOMAIN 102..263
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 32678 MW; DD0D5F5FF1EC996A CRC64;
MPWPKLWSSS PKGEDDSPES ISAKAGSTWE SATTTVAEAA QSVQRDTPEA VPAQLKAFTQ
PETIVAAVLL SATSLGFYRF YRSYLRRIPQ AININPGYLG RRSLVGQVTS VGDGDNFRMY
HTPGGRLAGW GWLPWRRVPL EKKALKDQTI HVRLAGIDAP EMAHFGRPSQ PYAQEALDWL
TAYLVGRRVR TYVYKADQYS RVVGTVYVWK GLFRRDVGLQ MLKAGYATIY EAKSGVEFGR
AKEARYRRAE WWAKAKRKGM WAGKKKDFES PREYKNRHGV GAPKEETKQ
//