ID A0A1V6SYY7_9EURO Unreviewed; 284 AA.
AC A0A1V6SYY7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404};
DE AltName: Full=Probable endonuclease lcl3 {ECO:0000256|ARBA:ARBA00014651};
GN ORFNames=PENSTE_c016G07192 {ECO:0000313|EMBL:OQE19091.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE19091.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE19091.1}.
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DR EMBL; MLKD01000016; OQE19091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SYY7; -.
DR STRING; 303698.A0A1V6SYY7; -.
DR OrthoDB; 208975at2759; -.
DR Proteomes; UP000191285; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT DOMAIN 88..255
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 32799 MW; FCB50C4B1FFF66CA CRC64;
MRWPPWSSES DSDESKKEKT TLSIFSRPAS TTNNPGSYLD WSAFLEPRTL IPTVLLTSGI
LLGIRFHRQY LRRIPDAPSI SPSFLRRRSI FGPVTSVGDG DNFRIFHTPG GKLAGWGWLP
WKRVPSNKKD LKNNTIHIRL AGVDAPELAH FGRPEQPFAR EAHVWLTGYL SNRRVRASVY
KQDQYNRVVA SVFVRRAFDF PPFRQRDVSY EMLRRGLATV YEAKVGAEYG GDAMEKKYRR
AEWWAKRRSK GLWKGYDKLG SNWESPREYK SRMGKNESAE NGRK
//
