ID   A0A3B4WF51_SERLL        Unreviewed;       864 AA.
AC   A0A3B4WF51;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein {ECO:0000256|PIRNR:PIRNR017179};
DE            EC=3.1.31.1 {ECO:0000256|PIRNR:PIRNR017179};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000002510.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000002510.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Endonuclease that mediates miRNA decay of both protein-free
CC       and AGO2-loaded miRNAs. {ECO:0000256|PIRNR:PIRNR017179}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC         phosphooligonucleotide end-products.; EC=3.1.31.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR017179};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR017179}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B4WF51; -.
DR   STRING; 1841481.ENSSLDP00000002510; -.
DR   Ensembl; ENSSLDT00000002612.1; ENSSLDP00000002510.1; ENSSLDG00000001950.1.
DR   GeneTree; ENSGT00510000047270; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016894; F:endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters; IEA:UniProtKB-EC.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:InterPro.
DR   CDD; cd00175; SNc; 2.
DR   CDD; cd20433; Tudor_TDRD11; 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   InterPro; IPR047386; Tudor_TDRD11.
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; 2.
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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          17..166
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          219..321
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          334..490
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          509..614
FT                   /note="TNase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50830"
FT   DOMAIN          683..741
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
SQ   SEQUENCE   864 AA;  96869 MW;  F14EF80861B6DCF0 CRC64;
     MASVSAPTQT APTPTAPLQR GIVKMVLSGC AIIVRGQPRG GPPPERQINL SNIRAGAMAR
     RAAQGQPDTK DTPDEPWAFQ AREFLRKKLI GKEVCFTVEI KTALGREYGM VYLGKDTTGE
     NIAESLVNEG LATVRREGIR GNNPEQARLC ELEDQSKSSK KGMWSEGGGT HTIRDMKYTI
     ENPRNFVDSL HQKPINDKMH ASLGQILTHF PLVAKYPLIE CPTFKREADG TETPEAFAAE
     AKFFTESRLL QRDVQIILES CPNQIILGTI LHPNGNITEL LLKEGFARCV DWSMAVYTQG
     AEKLRAAERS AKERKVRIWK DYVAPTANLD QKDRQFVAKV MQVVNADAMV VKLNSGEYKT
     IHLSSIRPPR IEGEEKNKDK DKRFRPLYDI PYMFEAREFL RKKLIGKKVN VTVDYIRAAT
     GPGEGTPAFP ERTCATVTIG GINIAEALVS KGLATVIRYR QDDDQRSSHY DELLAAEARA
     IKNGKGLHSK KEVPIHRVAD ISGVELTFLL SIECPRSSRN LPGGMQVAEP FSDEAMLFTK
     ELVLQREVEV EVESMDKAGN FIGWLHIEGV NLSVALVENA LSKVHFTAER SAYYKTLVSA
     EEGCRQRKEK IWANYEEKPV EEVVHLSEEK ERVANYRPVY VTEITDTLHF YSQDVETGGQ
     LESLMETMRA EIAAQPPVEG SYSARRGDYC IAKFADGEWY RARVERVESP AKVHVFYIDY
     GNREVVTSTR LATIPPAFST RTLPAQATEY AFAFILIPQD EDARADVVDC VVRDIQNSQC
     LLNVEYSGAT CPHVTIQFGD TKDDVGLGLV KEGLVMVDVR KEKYLQKMVT EYLNSQESAK
     SARLNIWRYG DFRADDADEF GYSR
//