LCL3_VERA1
ID LCL3_VERA1 Reviewed; 287 AA.
AC C9SI22;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Probable endonuclease LCL3;
DE EC=3.1.-.-;
GN Name=LCL3; ORFNames=VDBG_04704;
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985218; EEY18595.1; -; Genomic_DNA.
DR RefSeq; XP_003005098.1; XM_003005052.1.
DR AlphaFoldDB; C9SI22; -.
DR SMR; C9SI22; -.
DR STRING; 526221.C9SI22; -.
DR EnsemblFungi; EEY18595; EEY18595; VDBG_04704.
DR GeneID; 9530316; -.
DR KEGG; val:VDBG_04704; -.
DR eggNOG; ENOG502S1U4; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR Proteomes; UP000008698; 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..287
FT /note="Probable endonuclease LCL3"
FT /id="PRO_0000408686"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 88..246
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 287 AA; 32104 MW; C3CEFA8AD7571345 CRC64;
MPWPFGPSGS SEAPPPQKPR DDKVEGREPA KSWNSLLPKP DPPLQAAKEW APVFLTAVGS
LAAFMFYQSY LRRFAGAASI QENFFRKRSL LGRVTSVGDG DGFHLYHTPG GKLAGWGWLR
KIPEGRSNLK GETISIRLAG IDAPEGPHFG RPGQPFAAEA QAHLSKYILH RRVRAHLHKR
DQYNRIVATV STRQPFIKKD VGLEMLKQGL ATTYEAKSGV EWGGKESIYK AAEAKAKAKK
LGLWSIKASE FESPRDFKNR TQGNEKSERD VEGSTVQKPW WRRWLTG