ID LCL3_ASPTN Reviewed; 295 AA.
AC Q0CUT8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=ATEG_02546;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476596; EAU37508.1; -; Genomic_DNA.
DR RefSeq; XP_001211724.1; XM_001211724.1.
DR AlphaFoldDB; Q0CUT8; -.
DR SMR; Q0CUT8; -.
DR STRING; 341663.Q0CUT8; -.
DR EnsemblFungi; EAU37508; EAU37508; ATEG_02546.
DR GeneID; 4316848; -.
DR VEuPathDB; FungiDB:ATEG_02546; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 208975at2759; -.
DR Proteomes; UP000007963; 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 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 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; Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Nuclease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..295
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408648"
FT TRANSMEM 60..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 98..265
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 295 AA; 34200 MW; 9596D61398C50DF6 CRC64;
MRWPPWGSES QQADTPSPST EQQAQQPPTA PAARPSRPNK DWNQSVNAFD WAAFTELRTI
IPTAILTTAI LGIVHIHRRY LRRFPDAVSI APSYFRQRSI LGQVTSVGDG DNFRLFHTPG
GRLAGWGWLP WKKVPTSKKE LRDKTVHVRL AGIDAPELAH FGRPAQPFAR EAHQWLTAYL
MTRRVRAYVH RQDQYQRVVA SVYVRRALDF PPFRRRDVSY EMLRRGLATV YEAKAGAEFG
GPGMERKYRR AEWWAKFRGL GLWKGFRRNK EWESPREFKT RMGLEDQTQG RENKS
//
