LCL3_PICST
ID LCL3_PICST Reviewed; 235 AA.
AC A3GI61;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=PICST_29232;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000002; EAZ63178.2; -; Genomic_DNA.
DR RefSeq; XP_001387201.2; XM_001387164.1.
DR AlphaFoldDB; A3GI61; -.
DR SMR; A3GI61; -.
DR STRING; 4924.XP_001387201.2; -.
DR EnsemblFungi; EAZ63178; EAZ63178; PICST_29232.
DR GeneID; 4851960; -.
DR KEGG; pic:PICST_29232; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; A3GI61; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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..235
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408678"
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 59..217
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 235 AA; 26967 MW; CEAE0E5C6F5C74F2 CRC64;
MAPIPQNSST EVSLLHPKVL LLSAGITTTA FLSYKFHQRY VTRLRTYLDI TPKILDNQQK
LYGYVTRVGD GDNFRFFHTP GGVFMGWGWL RKIPTNRNQL KDETLMIRLC GVDAPERSHW
GKPAQPFSEE ALIWLSSYVG KRYVTVTPFS IDQYKRLVAR AQVWKWTGKK DVSAEMIRQG
LGIVYEGKSG AEFGDNEALY RNLEAKAKRQ KKGVWSLGKK MTTPGEFKRE HYRGD
