ID A0A016T3P2_9BILA Unreviewed; 670 AA.
AC A0A016T3P2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN Name=Acey_s0142.g2317 {ECO:0000313|EMBL:EYB97246.1};
GN Synonyms=Acey-xrn-1 {ECO:0000313|EMBL:EYB97246.1};
GN ORFNames=Y032_0142g2317 {ECO:0000313|EMBL:EYB97246.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB97246.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB97246.1}.
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DR EMBL; JARK01001478; EYB97246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016T3P2; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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; -; 1.
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:SF41; 5'-3' EXORIBONUCLEASE 1; 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; 1.
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 mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR037239};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 280..665
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT REGION 373..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 77322 MW; 204FE57561ED96E6 CRC64;
MGVPKFYRWI SERYPCLSEV ISDTEIPEFD NLYLDMNGII HNCSHPNDDD VKFRISQEQI
FADIFAYIDK LFNIIRPKKV FFLAVDGVAP RAKMNQQRAR RFMSARTAEE QLQAHLRKGE
ELPKEKRFDS NCITPGTLFM AELHNELSKW LETKVEKDQA WHGIRVYLSG HDCPGEGEHK
IMDFIRHERT LEGYDSNTRH CMYGLDADLL MLGICSHEPH FSLLREEVKF NRPAPKKGGA
AAPQRANPSQ INFHLLHLSL LREYLYWEFY PLKASLPFTY DIEHIIDDWV LMGFLVGNDF
IPHLPHVHIH DDALPLLYQT YIQVLPTLEG YINESGILNL QRFEVFLKAF AANDRRHFLQ
TLEDESFLRS KTGRDPHGLF KKEHTEEESP LSGAESSEEA DGSDEISPDD EAAFVSSDEE
DSSSDDIPDE LPDGGVESAA ELLSRLNADS DPGEDELTEA VMAAELRGMD DKEFENDVET
CWTKTVSNSF RRHKRLYYRE KMKYENITKS ELRKQAEGYV RAIQWNLHYY YKGCVSWNWF
YPHHYSPYIS DVVDFSNMDM SFDLGEPFKP FEQLLAVLPS ASAECLPSPF RDLMCNKESP
IADFYPTDFR TDLNGKKNDW EAVVLIPFID EARLLSAVQS KMPLLTPEEN ARNSIGEILL
FNFKTKGAQV
//
