ID A0A4Q4ZFZ9_9PEZI Unreviewed; 1330 AA.
AC A0A4Q4ZFZ9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=DL770_004943 {ECO:0000313|EMBL:RYP86351.1};
OS Monosporascus sp. CRB-9-2.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211643 {ECO:0000313|EMBL:RYP86351.1, ECO:0000313|Proteomes:UP000294245};
RN [1] {ECO:0000313|EMBL:RYP86351.1, ECO:0000313|Proteomes:UP000294245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRB-9-2 {ECO:0000313|EMBL:RYP86351.1,
RC ECO:0000313|Proteomes:UP000294245};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional protein that exhibits several independent
CC functions at different levels of the cellular processes. 5'-3'
CC exonuclease component of the nonsense-mediated mRNA decay (NMD) which
CC is a highly conserved mRNA degradation pathway, an RNA surveillance
CC system whose role is to identify and rid cells of mRNA with premature
CC termination codons and thus prevents accumulation of potentially
CC harmful truncated proteins. {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family.
CC {ECO:0000256|PIRNR:PIRNR006743}.
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:RYP86351.1}.
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DR EMBL; QJOA01000155; RYP86351.1; -; Genomic_DNA.
DR STRING; 2211643.A0A4Q4ZFZ9; -.
DR Proteomes; UP000294245; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR CDD; cd18673; PIN_XRN1-2-like; 1.
DR Gene3D; 1.25.40.1050; -; 1.
DR Gene3D; 2.170.260.40; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR047007; XRN1_D1_sf.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR047008; XRN1_SH3_sf.
DR PANTHER; PTHR12341:SF83; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF17846; XRN_M; 2.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006743};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR006743};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006743};
KW Nonsense-mediated mRNA decay {ECO:0000256|PIRNR:PIRNR006743};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR006743};
KW Reference proteome {ECO:0000313|Proteomes:UP000294245};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..192
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 240..490
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 502..599
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 648..836
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 840..1066
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1084..1154
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
SQ SEQUENCE 1330 AA; 150298 MW; F8DEE6775F8CD007 CRC64;
MNGIIHNCTH KDSHDTSFRL SEDEMFIRIF NYIEHLFGKI KPKKLFFMAI DGVAPRAKMN
QQRARRFRTA LDAEQAREKA IREGVELPKE DPFDSNCITP GTEFMAKLTR QLKYFINKKV
SEDSDWQGCD IVLSGHEVPG EGEHKIMEYI RNAKAQPDYS PNVRHCLYGL DADLIMLGLL
SHDPHFCLLR EEVTFGRPSK TKSKELEHQN FYLMHLCIVR EYLELEVQEL KQEGALKFPF
DMERIIDDFI LMAFFVGNDF LPNLPNIHIN EGALATMFRI YKQILPQCEG YINEGGVINL
PRLGLLLEQL SKEEYRHFEH EHADSKWLKS KQLTGASGEE MGRAKGKLVM TSPQKELWKK
IRKFVHKRST QPLDLGSRLN AADRKFVQDV AENLHIEWRT VEDDDGQRHL LLSFPAKPDG
ADEEEEEEEE GHLALLRVTK RYDKAQVVDV SAEEAQATMQ AKYKEKFLEW KEKYYAGKFE
WTPENKVTEL RKLYVEKGFN ADLNFKLGQP FRPFEQLMGV LPDRSKKIVP SVYQDLMTDP
KSPIIDFYPR DFELDMNGKK MEWEAVVKIP FIDEERLLSA MAPRNELLSP DEKARNDFGV
SLKFTYDPNV NFTYPSSMVG VFPDVRYCHC TENIFDLPTT DGLELYVGLK DGAKLGVDAL
AGFPSLATLP YNAALGFHGV SVFQQESRNE SMVVTLADVE MRSRVESAKV KLGQKCYVGY
PFLQEAKIVR VSDELFDYTL AQDGSGQVVQ THHSGKDIED WNKKASRIEN FYSKRLGIIT
GPVESMVHVD MLKGLMKTDE GATIKQYGMI PGMETDYAAQ VIVDEVVSED ERFIERAAIP
LDEEFPVGSR VFFLGDYAYG RPVQVEGHSN NRADVRILIP QVKEPEFARP IIDRAERENQ
YRPSYAVAKD LGLHPLILSK IMSAFHVNTI GGNIRVNLGL NLKFDARKQK VLGYSRKSNT
GWEFSPAAIK LLTEYMQKFP DFFAALLQNP QGKELDETDL WPDQNVATAK IKEIGQWLKS
IETSKFERVP LDAEQLDSDV VMELQRAVDA IKEASSKVDF KKLNGVPRSA LLQPKDAEQR
LGSQKFRLGD RLVYVHAAGK VPIASKGTVV GISEIGSHHM LDVLCDYAFM NGTTLGGRCD
PFRGQTVPAN SVLNLTNKQV VAFSKTSWER RPAQPPTMPL QPGGYGAGRG QLRDATAPAP
LRGTPTVFLI FSIAALFIDQ CQMETRSNSL MEVLVETEGA RGAIVLDEDT EVVGVTLVLP
QPRPTRTLII LDCQRAQAPF LGSRITPSHR PLALIPAVVG VDVGVDVEEV MAGALEARLQ
LDRIVAALDL
//
