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Database: UniProt
Entry: A0A167BG44_9PEZI
LinkDB: A0A167BG44_9PEZI
Original site: A0A167BG44_9PEZI 
ID   A0A167BG44_9PEZI        Unreviewed;       270 AA.
AC   A0A167BG44;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404};
DE   AltName: Full=Probable endonuclease lcl3 {ECO:0000256|ARBA:ARBA00014651};
GN   ORFNames=CI238_00420 {ECO:0000313|EMBL:KZL81292.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL81292.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL81292.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL81292.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL81292.1}.
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DR   EMBL; LFIW01001670; KZL81292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167BG44; -.
DR   STRING; 1573173.A0A167BG44; -.
DR   Proteomes; UP000076584; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..240
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  30117 MW;  3BE13B2C5AA5DC92 CRC64;
     MPWPFSSSSS PTPSKTEDGA HSKSTSWNDL LPKPDPPLQA AKEWAPVFLT SVASLAAFIF
     YQSRLRRFPT AGHIQPDLFR KRTLLGRVTS VGDGDNFHMF HTPGGKLAGW DWLRKVPTTK
     VALKGKTIPV RMAGIDAPEG AHFGRPGQPG AAEALQWLRS YILGKRVWAR IHRRDQYERV
     VATVYVRRFL FKKDVGLEML KLGLATTYEA KSGVEWGGAE EVYKAAEAKA KAKKLGIWNG
     KASDFESPRA YKSRTNEAEV KKSGWFSGWL
//
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