ID A0A2T0FHM8_9ASCO Unreviewed; 1440 AA.
AC A0A2T0FHM8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=B9G98_02114 {ECO:0000313|EMBL:PRT54494.1};
OS Wickerhamiella sorbophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT54494.1, ECO:0000313|Proteomes:UP000238350};
RN [1] {ECO:0000313|EMBL:PRT54494.1, ECO:0000313|Proteomes:UP000238350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS02 {ECO:0000313|EMBL:PRT54494.1,
RC ECO:0000313|Proteomes:UP000238350};
RA Ahn J.O.;
RT "Genome sequencing of [Candida] sorbophila.";
RL Submitted (APR-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:PRT54494.1}.
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DR EMBL; NDIQ01000021; PRT54494.1; -; Genomic_DNA.
DR STRING; 45607.A0A2T0FHM8; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000238350; 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:SF80; 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:UP000238350};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..226
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 276..664
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 720..891
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 895..1116
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1141..1211
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1230..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 162498 MW; 8653386DE35D323D CRC64;
MGIPKYFRYI SERWPTISQL VNDSVIPEFD NFYLDMNSIL HTCTHKDNDP THVLSEAEMY
VAIFNYIEHL VATIKPKSVL YMAIDGVAPR AKMNQQRSRR FRSALDQETA RRKAIESGVE
LPKEDPFDTN AITPGTEFMA KLTVQLKYFI HRKVTEDADW QDIRVVLSGH EVPGEGEHKI
MNFIRSLASD ENYNSNTRHC LYGLDADLIM LGLSTHQPHF SLLREEVFFG RSERFQSAEL
SEKRFFLLHL SLVREYLQLE FRNVLESGDD ETQPSQFDFE RILDDFILIN FFIGNDFLPE
LPLLLIKDGA IPEIMDTYMR YLSKVKDYIT ENGKLNFANL KLWLKEMAQY QYQRFEEEAV
DAEWLNNQLE LVSNVNTDEP ETLILTPSQR DIVRVMKPFI LNSVLADDPT SEEFEVSEVL
DESSNIFDRK FVELLAQQTG FIVQDGIITL ESIPGDKRQW VSDTRKILRV YEKAQISSAE
DDLNRQALYD SKFNQWSDRY YRSKFGVRHD DPKVKEVVRN YLEGLQWVLG YYYQGCPSWS
WYFHGHYAPM IVELFNGITL DFKVEFGPSR PFLPFEQLMG VLPDRSSKLV PAAYRDLMSS
PQSPIIDFYP NEFQLDLNGK KADWEAVVLI PFIDEKRLID ALTPRENRLT EAERARNIYG
SDLEFTYTPQ SSYFYPSSMP GVVPDLPACA VAVLSINPHD KSYAETYYAR DRSDDPKFAY
MAGFPTLKTL DWQFEIEKAH VRVFEYDARN ESIILHIKND YSSQTIKELV ALIGESAYVD
WPFLREAKIT GVSNRDVYFS SRKGSGTPHD ARVSQLWSKQ LPTIKRNYES RGVDLGSVDV
LVHYQPLVGL LRKTDGSYVK EFNNDIKTEK VLPVQLLVED IEEEDERFKE REPIPVADEY
PVDSRAVLLM NRHYGAPVTV TGHTDTAINV EALALTDPEP QFGNQVASRE KSTYQYFSAR
EVADSLGISF AFLSRLTSRF MFVLKNEKIN LGLVLKRPAQ NLKASGYTRM GFKGWEYSQK
GLLLILAYLK SFPVILQALA SAPQSNTGIP DLRKVLPESI SSEEIAHQVR SMKTWLNENA
SKIQFVPMND ETLSDEGIAQ IEKWAVEYSK KPIQAHKIQI SKLPRAALLT PASAHHQLRR
QKFFLGNRVV SAVDFGKVPL YARGTVVGIN EGASHRTLNV VFDAEFGAGS TLDQRVKTKR
GLVVQAGTVI NLTFKQLAYD RNQDNDVLVP AVPQARSTKR VDTRQRNLKP APVSQSVWTK
AKPAPAGPAS KAPAGSAPKA PAGPPVRPAA ADMFLPPVSA SASAESAELM AALKGTTKTK
AESPGSGVPS APKGPKKDAS HKAQGEAKQK KQTSPKVPKA HKAPKAPKAA KESEPEPTEP
KAPKARQAPK EPEATKSTPP TPAPTPAAPD VLGSYVQHAT ENAGRKRQGV SDLLASLKMQ
//
