ID A0A0N4U8P4_DRAME Unreviewed; 899 AA.
AC A0A0N4U8P4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=DME_LOCUS295 {ECO:0000313|EMBL:VDN50322.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000342901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000342901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN50322.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Plays a role in
CC maintenance of steady-state concentration and turnover of microRNAs
CC (miRNA) by degradation of mature miRNA. Degradation role is enhanced
CC when in complex with paxt-1. Partially redundant to xrn-1 in miRNA
CC guide strand degradation. Implicated in differential regulation of
CC mRNAs such as let-7 by controlling the accumulation of mature miRNA.
CC Positively regulates molting of the pharyngeal cuticle.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
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DR EMBL; UYYG01000002; VDN50322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4U8P4; -.
DR STRING; 318479.A0A0N4U8P4; -.
DR WBParaSite; DME_0000342901-mRNA-1; DME_0000342901-mRNA-1; DME_0000342901.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341:SF77; 5'-3' EXORIBONUCLEASE 2; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 2.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR037239};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR037239};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..257
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 326..782
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 879..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 104621 MW; 998876F06BFE57FF CRC64;
MGVPAFFRWL TRKYPSIIVN AVEEKKREID GTVLPVKTME PNPNFQEFDN LYLDMNGIIH
PCTHPEDRPA PKTENEMFAL IFEYIDRLFA IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
AAKDASEKEA QIEEVRKALE TEGFPLPPKK TNEERFDSNC ITPGTPFMSR LLLADALRYY
IYLRLNSDPA WSNIMVILSD ANVPGEGEHK IMDYIRRQRA SSTHDPNTAH CLCGADADLI
MLGLATHEPN FTIIREEFVT NQPRPCEICG QYGHILMDCR GLIQQEIPDY QCTPLQKETN
FIFIRLPILR EYLEKDLQIS NSPVAFDLER AIDDWVFMCF FVGNDFLPHL PSLEIRENAI
DRLIKLYKDM IHETRGYLTN AGEVNMERVQ IILDNLGAVE DEIFKTRQTR EIEMRRNKMI
RNEKRSTNVL AYVPSSGSLI TPEPGVPLSF NGCDTRLMAR DSRMQALNYQ LHSQSEKKKM
DCKRKMEYDS DSDEPYDEVR LWESGWKERY YRSKFQVDGN DLGFRKKIAW AYATGLCWVL
KYYYQGCASW DWYFPYHYAP FASDFDLITQ FKVDFDKPTQ PFKPLEQLMA VFPAASRSHL
PESWQHLMVD PESPIIDFYP DDFVIDLNGK KFAWQGVALL PFVDEKRLLE TLKEVENALD
DCEKTRNSRG SDRLFVGSKH PLCKFLEEMY SSVDSDNSFI QIDTLLTLGV DLNVAPDPDG
CLLGESYLSP VPFEQFGDIK VKPNRALMVI CQDPQFEKGK IFSANRLPGA VDLPRTLKPE
DWNNRIPYRP QIGFSRNVPR AFLGEPGHRM LVHETKRFHA HVRNVQAYRP RWQSTYVGSG
DVYRFNSSSL DPYWQSCPRV EMHRFRSFEG FYPQSSSLFH EEGPRSNVRP RRPQFFQRN
//
