ID A0A2Z6Q956_9GLOM Unreviewed; 1374 AA.
AC A0A2Z6Q956;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=RclHR1_01160026 {ECO:0000313|EMBL:GBB85032.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB85032.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBB85032.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBB85032.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) 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:GBB85032.1}.
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DR EMBL; BEXD01000180; GBB85032.1; -; Genomic_DNA.
DR STRING; 94130.A0A2Z6Q956; -.
DR Proteomes; UP000247702; 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; 2.30.30.750; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
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:SF41; 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; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 1.
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:UP000247702};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..223
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 269..660
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 706..890
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 894..1129
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1150..1216
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 158163 MW; 8A343424B44AC29B CRC64;
MGIPKFFRWM SERYPLCSQL ITENRIPEFD NLYLDMNGII HNCSHSNDTD VHNVSEDKIF
LEIFNYIDHL FTKIKPKQLF FMAVDGVAPR AKMNQQRARR FRTAAEAAKK AESRGEESPQ
EAPFDSNCIT PGTEFMAKLS RQLKYFINKK VSEDSNWRDI KIVLSGHEVP GEGEHKIMEY
IRNTKAQEDY NPNVRHCLYG LDADLVMLGL LSHDPHFALL REEVTFGSSR KKKQGRVESQ
NFYLMHLSLL REYLDLEFSI LKDTLPFEYN LERIIDDFIL LALFIGNDFL PHLPNLHIAE
GALGLMFQVY KKVLPDAGGY INDGGILEMK RLEMIFKELT IFERDVYEGE FVDLKWFKGK
QKRNLEMMEE KKRVEKLVLT PKQREIYNKI KKLVKARTGS IHFPADYPAR DRVFIKNLAK
ALKIHQSVLE DGENGENKHL YVECDFEEES SEGTSEMREE VYEKYETAEI IEEDDIETYE
EKERKKDEGA FIEWKKKYYM EKMQIDYDDP ESMDKIVSSY VEGLQWVLWY YYFGVASWGW
FYPYHYSPKI SDLYELERFD ILFDKDDSPF TPFEQLMGVL PEGSKRFLPK AYQDLLSDPN
SPIIDFYPRE FTTDMNGKKQ EWEAIVNIPF IDQRRLIAAL KDRKDQLTEE EKERDTFGDI
YVFTYDPDHK EPYPSSLPGF FPDIHYCLCH TEVYHVPTLE GPIVKGLCDG VQLGVKAMAG
FPSLQTLQHT AKLLHHGVNV FNSESKNETM VISIVDQFKD MNTIDIVHEK VGKRIFIGWP
FLQEGKVQAI SDEQFRYELS HNGQITSIPH KSDVADQWRR KADKFEQVNS KRFGTIIGKV
NVLAHVLVLK GLKQMQDGAL VRDFVEEEQD CAIQTTVDSV ECEDSRYEEK PAVPLAEAFP
INTKIFYLGS SYYGCPGAVS SNTEENLAVR LIIDKNNVNE TEFGSEIAKT FAARIRYSPS
YSVAKRLNIS GLTLSKLTAS LHVICKSNSN EQKSTDQRIN LGLNLKFEAK KQKVLGYTRK
TKTKDKDGWE YSEKAIQILA EYKEKFPEFI QALENKHDKD EIYTAEDFYP KEEAVSKIHA
IKDWLKTVEV RDFEKVPLEA EQLDKEAIQD IEEAANELLE NKDTDQVEKE KLARHKLLKP
SHASTLLQNQ KFNLGDRVVF VKDSGNVPIA SKGTIVGIEK NNIDVVFDCT FMGGSTLGDR
CSNYRGMTVP ANSLLNLTRP QLPDRRLNTG NGRSRHGTNF NNHQTRYQEA LQNGQQTHYN
SNAYPYYYNN GYSSRGRGWP AIVSNGSHQR SNRPRGVSGS NGYIQSQLHA RPISQSQASS
GATKYNVQNQ THHTYRNPRS SNMNGYLPSR GNGSRVHFGG NGVSRGRGRG DGKT
//
