TRIMR_BOMMO
ID TRIMR_BOMMO Reviewed; 532 AA.
AC H9JAQ7;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Pre-piRNA 3'-exonuclease trimmer {ECO:0000305|PubMed:26919431};
DE EC=3.1.13.- {ECO:0000269|PubMed:26919431};
DE AltName: Full=PARN-like domain-containing protein 1 homolog {ECO:0000303|PubMed:26919431};
DE Short=BmPNLDC1 {ECO:0000303|PubMed:26919431};
GN Name=PNLDC1 {ECO:0000303|PubMed:26919431};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAPI, AND MUTAGENESIS OF
RP GLU-30.
RX PubMed=26919431; DOI=10.1016/j.cell.2016.01.008;
RA Izumi N., Shoji K., Sakaguchi Y., Honda S., Kirino Y., Suzuki T.,
RA Katsuma S., Tomari Y.;
RT "Identification and functional analysis of the pre-piRNA 3' trimmer in
RT silkworms.";
RL Cell 164:962-973(2016).
CC -!- FUNCTION: 3'-5' exonuclease that specifically cleaves precursor piRNAs
CC (pre-piRNAs) at their 3' ends (PubMed:26919431). Trims pre-piRNAs to
CC their mature size, a process required for piRNAs maturation and
CC stabilization, and subsequent pre-piRNAs 2'-O-methylation
CC (PubMed:26919431). The piRNA metabolic process mediates the repression
CC of transposable elements during meiosis by forming complexes composed
CC of piRNAs and Piwi proteins and govern the methylation and subsequent
CC repression of transposons (PubMed:26919431).
CC {ECO:0000269|PubMed:26919431}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:26919431};
CC -!- SUBUNIT: Interacts with Papi/Tdrkh; interaction takes place on the
CC mitochondrial surface and recruits PNLDC1/trimmer to PIWI-bound pre-
CC piRNAs. {ECO:0000269|PubMed:26919431}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:26919431}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; BABH01008568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BABH01008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004930511.1; XM_004930454.2.
DR AlphaFoldDB; H9JAQ7; -.
DR SMR; H9JAQ7; -.
DR STRING; 7091.BGIBMGA006602-TA; -.
DR GeneID; 101738496; -.
DR KEGG; bmor:101738496; -.
DR eggNOG; KOG1990; Eukaryota.
DR HOGENOM; CLU_018030_2_0_1; -.
DR InParanoid; H9JAQ7; -.
DR OrthoDB; 1402758at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:1990511; P:piRNA biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.30.420.10; -; 2.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF04857; CAF1; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Exonuclease; Hydrolase; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nuclease; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Pre-piRNA 3'-exonuclease trimmer"
FT /id="PRO_0000439352"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MUTAGEN 30
FT /note="E->A: Catalytically inactive mutant; strongly
FT reduced trimming reaction."
FT /evidence="ECO:0000269|PubMed:26919431"
SQ SEQUENCE 532 AA; 61318 MW; 32019493563CFFDB CRC64;
MDITKENYYE ELDNIAKNIK DSCFISFDAE FSAILTKESF KYSLFDTNEE RYNKYKTQIS
TMKMMQVGLT MFQYDRELDA YLATGYTFHL CPQLIGTINQ SLIFQASTLK FLCKHNFDFN
KFIYEGLPYL SKSDEALLNR YRIENNLFDY VSESLEFDEE KQINQCSSEV SKWLSSSIED
TMYLDIDNAI CRYLLHLELR QRYPGILTTD SLGNSKKILI YRDKNVEGAK NAPIAILEDN
LIAYLLGFLH VIKLLETHKK PIVGHNMFLD MLFLHNQFIG PLPDSYTMFK KNINSVFPTI
FDTKYISHAM SKKLTFSESW KSNALQDLYE FFAERKCKKL EYGINIVRLT TPFDIKQSYH
EAGWDAYCSG YCFIRLGHWA ACENRGKSHV IGPREKLAAL APYCNKVNVI RGGVSYMNFS
ENDPPRNRPV LLHVKCLKDT VIDVEKVASL LGSFGSIDIK PCGKRAALVA TGAQFMVDKI
LKTYENNRDY RISKYSVYKH SVAGRFAIWS GSIVTGGLAL YLIHKKFKSI LL
