ID A0A0D2CD17_9EURO Unreviewed; 878 AA.
AC A0A0D2CD17;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404};
DE AltName: Full=Probable endonuclease lcl3 {ECO:0000256|ARBA:ARBA00014651};
GN ORFNames=PV06_00469 {ECO:0000313|EMBL:KIW47807.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47807.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW47807.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47807.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR017179}.
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DR EMBL; KN847332; KIW47807.1; -; Genomic_DNA.
DR RefSeq; XP_016268023.1; XM_016400970.1.
DR AlphaFoldDB; A0A0D2CD17; -.
DR STRING; 215243.A0A0D2CD17; -.
DR GeneID; 27352543; -.
DR VEuPathDB; FungiDB:PV06_00469; -.
DR HOGENOM; CLU_005966_1_0_1; -.
DR OrthoDB; 375531at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:InterPro.
DR CDD; cd00175; SNc; 1.
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; 5.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 5.
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 Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT DOMAIN 2..139
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 162..303
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 312..449
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 478..611
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT DOMAIN 695..755
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 338..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 97624 MW; 32B9F6F4FD393A73 CRC64;
MALLQARVKS VLSGDTLIIT NQKGAERTLS LAYISAPRLK REGDEPFAFQ SREFIREQCL
GKVIQFQVLY AIPTTKREYG RVKLPTGVEL PDLIVQEGWA KVREDAGKKE DDENALAYLD
KLRTLEGEAK SEGKGVWGKG GHIETSSEVA DPNALVEQYK GKKIDAIIER VLTGDRLIAR
VMLTPTKHVQ TMLVMAGIRT PATKRTSPEG KDIPAEPYGT EAHTFVEERL HQRKCAVELL
GVTPQNQLIA NVLHPKGNIA KFLLEAGLAR SNDQHVTLLG NEMSQFRQAE NAAKTARRGI
FTGVSSKAAG VQEADFTVSR VLNAETVFIR TRSGEERKVT LSSIRQPKPS DPKQAPFGAD
AKEFLRKRLI GKHVKVSIDG KRPASEGFEE REVATVIING KNIALTMVEA GYASVIRHRR
DDDDRSPDYD ALLLAEETAQ KEEKGMWSPK APAAKKYQDY SESLQKAKME ASVLQRQKKV
PAVVDFVRAG SRFVVLVPRE NAKLTFVLSG IRTPKPARQP GDASEPFGQE ALDFASRRCM
QRDVEIDVEN TDKVGGFIGT MYVGRENFAK TLVEEGLASV HAYSAEQSGH ANELVAAEKK
AKEGRKGMWH DWDPSQEQEE QAEEAPLPTN GTNGTNGEST ERRKDYRDVM VTHVDEAGKL
KIQQIGSGTT GLTELMNAFK SFHLNKANDT PLPGPPKVGD VVAAKFTLDN EWYRAKVRRV
DREGKKVDVT YLDYGNSETV PWSRLRPLTQ PQFSTQKLKP QATDAVLSFL QLPTSQQYLR
DAVDFVMEQT EGRELVANVD YVAPEGTLYL TLLDPKVSSK IDESINAEVV REGLAMIPTK
LKAWERQSAD TLTQLRALQD QAKEARRGMW EYGDLTED
//