ID   EXD1_XENLA              Reviewed;         444 AA.
AC   Q6NRD5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=piRNA biogenesis protein EXD1 {ECO:0000305};
DE   AltName: Full=Exonuclease 3'-5' domain-containing protein 1 {ECO:0000250|UniProtKB:Q8NHP7};
DE   AltName: Full=Exonuclease 3'-5' domain-like-containing protein 1 {ECO:0000250|UniProtKB:Q8NHP7};
DE   AltName: Full=Inactive exonuclease EXD1 {ECO:0000305};
GN   Name=exd1; Synonyms=exdl1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding component of the PET complex, a multiprotein
CC       complex required for the processing of piRNAs during spermatogenesis.
CC       The piRNA metabolic process mediates the repression of transposable
CC       elements during meiosis by forming complexes composed of piRNAs and
CC       Piwi proteins and governs the methylation and subsequent repression of
CC       transposable elements, preventing their mobilization, which is
CC       essential for the germline integrity. The PET complex is required
CC       during the secondary piRNAs metabolic process for the piwil2 slicing-
CC       triggered loading of piwil4 piRNAs. In the PET complex, exd1 probably
CC       acts as an RNA adapter. Exd1 is an inactive exonuclease.
CC       {ECO:0000250|UniProtKB:H9IUR0, ECO:0000250|UniProtKB:Q8CDF7}.
CC   -!- SUBUNIT: Homodimer (By similarity). Component of the PET complex (By
CC       similarity). {ECO:0000250|UniProtKB:H9IUR0,
CC       ECO:0000250|UniProtKB:Q8CDF7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:H9IUR0}.
CC       Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC       specific organelle required to repress transposon activity during
CC       meiosis. {ECO:0000250|UniProtKB:H9IUR0}.
CC   -!- DOMAIN: The 3'-5' exonuclease domain lacks the conserved Asp-Glu-Asp-
CC       Asp (DEDD) residues that coordinates divalent ions essential for
CC       exonuclease activity. {ECO:0000250|UniProtKB:Q8CDF7}.
CC   -!- SIMILARITY: Belongs to the EXD1 family. {ECO:0000305}.
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DR   EMBL; BC070821; AAH70821.1; -; mRNA.
DR   RefSeq; NP_001084849.2; NM_001091380.1.
DR   AlphaFoldDB; Q6NRD5; -.
DR   SMR; Q6NRD5; -.
DR   BioGRID; 101261; 1.
DR   IntAct; Q6NRD5; 1.
DR   DNASU; 431895; -.
DR   GeneID; 431895; -.
DR   KEGG; xla:431895; -.
DR   CTD; 431895; -.
DR   Xenbase; XB-GENE-993344; exd1.L.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 431895; Expressed in testis and 9 other tissues.
DR   GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR   GO; GO:1990923; C:PET complex; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Meiosis; Reference proteome; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN           1..444
FT                   /note="piRNA biogenesis protein EXD1"
FT                   /id="PRO_0000337247"
FT   DOMAIN          142..205
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          49..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  50781 MW;  678C4CD5CEBD5065 CRC64;
     MLINKVKDLE TGKIIPGAQL LFGYNILNVA LQKDVEEVPA KHLDKLTIED REQTSTEQRH
     ADECNQDAER THRDIDKSQD LRTRTLKVIK HSVDEEEVGY TIIDQFQPIF GPAIRHLQNQ
     KVISIGAVGQ NICRHGKLSW LQFATRSRVY LFDVLVLGSK VFKNGLQMVL EDKGILKVIH
     DCRWLGDILS HQYGIILNNV FDTQVGDVYL FSMETGGFLP HGTRTLEECL IHHLSMLPSK
     VSFLAHRQTL TKEYHDIWFD RPMDPTLLKL LSLEVTYLMP LRSAMLDAMF SDFTLLVDGY
     LNAYRRGTAD ILESPELSVA ELPKELQQLR VLQQMRREKA LKEYDVNNKG LLTRVEAEKA
     PRSEASGTKH DAELENVVKL TKSEKSFHQT MTTNAPLLEN QTEKQQGALC QKFPVVPNCF
     PRGPFDYYLY KKWASNDTPT TNVS