ID A0A1E1KMM2_9HELO Unreviewed; 961 AA.
AC A0A1E1KMM2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404};
DE AltName: Full=Probable endonuclease lcl3 {ECO:0000256|ARBA:ARBA00014651};
GN ORFNames=RCO7_08878 {ECO:0000313|EMBL:CZS98114.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZS98114.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZS98114.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZS98114.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR017179}.
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DR EMBL; FJUW01000014; CZS98114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1KMM2; -.
DR STRING; 914237.A0A1E1KMM2; -.
DR InParanoid; A0A1E1KMM2; -.
DR OrthoDB; 375531at2759; -.
DR Proteomes; UP000178129; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:InterPro.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR PANTHER; PTHR12302:SF2; STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00565; SNase; 4.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 4.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 5.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017179};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 84..223
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 247..390
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 400..537
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 566..699
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 778..838
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 17..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 106864 MW; 89AFEE9EEA61B20E CRC64;
MSDRPIKIGW DLNGALRKAA SGSKSSKSSR GSKGHKNEVK SQKVANVIET ALHPLIQAFP
APKIPPLGKH LIPNVPPARY VNMVLNQAKV KSVLSGDSVI LCSIAHPDRE RTLSLAYCTS
PHLKKEGDEL WAYESRDALR ELLVGKIVQF SVLYTIPNTK REYGVIYLND GRKLPEEMVK
NGWLKLREDA GRKEDSEEAL QQLDQLRLLE AKARADDLGL WSPNPNRIDV QHDMGDAPAW
LEKYKGQTLD GLVERVLSGD RMLVRVILSP TKHVQIMTLV AGIRAPTTER VNPSNKQTQP
AEEYGNEARQ FIEERLLQRN VKLDILGLSP QNQLIAAVKH PRNGTIAKFL LEAGLARCTD
FHSTLLGSEM SVLREAEKVA QQGKRGVYKD HVAKAATAGG NLEAQVTRVF SADVIYVRNR
AGVEKRISLS SVRGPRPTDA AEAPFRDEAK EFLRKKIIGK HVRLSIDGTR PATEDYDAKE
VASITYNDQN IGLQLVSAGW CSVIRHRRDD TDRAPNYDEL LAAQEKAKEE LKGMWSGKPA
KAKQYTDASE SLQKAKMHLP GLQRQKKVPA IVDFVKGGSR FVVLIPRDSI KLNFVLGGIR
APKSARGPND KSEPFGQEAH DLATKRLTQR DVEVDVHSID KVGGFIGELY INKESFAKIL
VEEGFATVHA YSAEQAGNAT ELLGAEQRAK DAHRGLWVDW DPSLDAAEED HTPTNGSNGD
AIIPRQADYR DVMVTHIDES CKLKLQIVGT GTSALETMMT QFKAFHMNPA NNTGLPGPPK
TGEFVAAKFT EDGSWYRARI RANDRTAKEA EIVYIDYGNS EKMPWSKLRP LSQPQFSTQK
LRPQAVDAVL SLMQFPTNVD YLQDAVSYIT DATAGAHLVA NVDYTAPEGT LYVTLYDEKT
STDLKQSINS DIVAEGHAMV PRKLKPWERG FGDVLKNLRE KEEQAIQDRR GLWEYGDLRE
D
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