LCL3_FUSV7
ID LCL3_FUSV7 Reviewed; 267 AA.
AC C7YQ31;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=NECHADRAFT_78963;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698898; EEU46398.1; -; Genomic_DNA.
DR RefSeq; XP_003052111.1; XM_003052065.1.
DR AlphaFoldDB; C7YQ31; -.
DR SMR; C7YQ31; -.
DR STRING; 140110.NechaP78963; -.
DR EnsemblFungi; NechaT78963; NechaP78963; NechaG78963.
DR GeneID; 9673414; -.
DR KEGG; nhe:NECHADRAFT_78963; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR InParanoid; C7YQ31; -.
DR OMA; IYHTPGG; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000005206; Unassembled WGS sequence.
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..267
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408668"
FT TRANSMEM 47..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 85..243
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 267 AA; 30177 MW; 2DCD937E332C88E4 CRC64;
MVWPFGSQSS DKGNEGKPQE QTKRSAVSWT RSLGSPDPDP FAAAKEWAPT VLFSLTGLAA
LQLYANYLRR IPGAAYVRPN FFRNRSLFGR VTSVGDGDNF HFFHTPGGRA VGWGWLRKVP
ESRKELRGRT IPIRIAGVDA PEGAHFGKPA QPFAAEALDW LTNYILNRNV RAYIYKRDQY
ERVVATVYVR RFLFRKDVGL EMIKRGLATT YEAKSGAEFG GMKEVYEKAQ AKAKRKRKGM
WSGKASEFES PREYKTKWAA HDKSNSS