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Database: UniProt
Entry: G0S7R0_CHATD
LinkDB: G0S7R0_CHATD
Original site: G0S7R0_CHATD 
ID   G0S7R0_CHATD            Unreviewed;      1461 AA.
AC   G0S7R0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN   ORFNames=CTHT_0028500 {ECO:0000313|EMBL:EGS21010.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS21010.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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}.
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DR   EMBL; GL988041; EGS21010.1; -; Genomic_DNA.
DR   RefSeq; XP_006693306.1; XM_006693243.1.
DR   STRING; 759272.G0S7R0; -.
DR   GeneID; 18256888; -.
DR   KEGG; cthr:CTHT_0028500; -.
DR   eggNOG; KOG2045; Eukaryota.
DR   HOGENOM; CLU_001581_1_2_1; -.
DR   OMA; VASWPWF; -.
DR   OrthoDB; 167745at2759; -.
DR   Proteomes; UP000008066; 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; 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:UP000008066};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT   DOMAIN          1..227
FT                   /note="Xrn1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03159"
FT   DOMAIN          275..669
FT                   /note="Xrn1 helical"
FT                   /evidence="ECO:0000259|Pfam:PF17846"
FT   DOMAIN          718..906
FT                   /note="5'-3' exoribonuclease 1 D1"
FT                   /evidence="ECO:0000259|Pfam:PF18332"
FT   DOMAIN          910..1136
FT                   /note="Exoribonuclease Xrn1 D2/D3"
FT                   /evidence="ECO:0000259|Pfam:PF18334"
FT   DOMAIN          1154..1224
FT                   /note="5'-3' exoribonuclease 1 SH3-like"
FT                   /evidence="ECO:0000259|Pfam:PF18129"
FT   REGION          1262..1461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1317..1335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1443..1461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1461 AA;  163834 MW;  1DC0D3E70FFB648A CRC64;
     MGVPKFFRWL SERYPAISQL IAENRIPEFD CLYLDMNGII HNCTHKDVDD VHFRLTEEEM
     FIAIFNYIEH LFGKIKPKKL FFMAVDGVAP RAKMNQQRAR RFRTALDAER AREKALREGK
     ELPKEEPFDS NCITPGTEFM AKLSLQLKYF INKKVSEDRD WQGPEIVLSG HEVPGEGEHK
     IMEYIRNARA QPDYNPNTRH CLYGLDADLI MLGLLSHDPH FCLLREEVTF GRQAKHKSKE
     LEHQNFYLLH LCIVREYLEL EFQELKEPGA IPFPFDMERV IDDFILMAFF VGNDFLPNLP
     RLHINEGALA LMFKIYKKVL PKCDGYINEN GKVNLDRLKI LLEELEQEEY RFFEQEHEDT
     KWLQGKKMLE NNEAEQAKAK AKGKLIISPS QKALWKQKIR KWLLNSTSPT LDLGADLNAA
     DRKFVEDLAE AAHIEWATKP DDDGIRHLVL SRPVMDEDDE EDEEAHAALY RIAKRYDNAQ
     VLDLSSEEAK AAVQEKYKQK FQEWKDKYYL SKMDGWTPQN LEQELKKMAE NYVQGLQWVL
     YYYYRGIASW PWFYGYHYAP MISDVVKGLG ADLNFKLGQP FRPNEQLMGV LPDRSKKIVP
     KVYWDLMTDP NSPIIDFYPR EFELDLNGKK MDWEAVVKIP FIDEKRLLEA MAPRNALLTE
     EEKARNEFGV PLKFTYSEDV DFVYPSSLVD VFPPIFHCHC VENIFDLPPM EGLEYRAGLA
     EGALLNVEAL AGFPTLATLP YTASLAFHGV NVFQQESRNE SMIVRLTDSH LRTKIDTAKV
     KLGQRCFVGY PFLQEAKVVA VSDELFEYTL ASDGSGQVIE RHHTPREIEE WKKKAERIEN
     FYSKRLGILI GPVESLVTVH MLKGLRKTDE GATVKEYGEV PGMETDYAAQ IIVDEVVNED
     ERFIEQAALP IEEEFPVKSN GFFVGDYNYG QPLEVVGYTK DGKLSIWLAV PTAREPEFAK
     QIIHEAHRSQ LYQPSYMVAK QLGLHPLTLS KITSSYYVRT VGDLRVNLGL NLKFESKKQK
     VLGYSSKSAT GWEFSQAAVL LISEYMRRFP DFFAAIVKNP SGSELNETDL FPDPAYATAR
     VKEIGAWLKT LKTSSMERVP LDAEQLDSDV VMRLAAKADE LGLGNQQTVS KKMNGVPRNA
     VIRPEDAEHR LGNQVFSLGD RVVYVARKGK VPIAFRGTVV GISRTPTNKL IDVVFDVTFL
     SGTTLGDRCP PFRGQTVPSN VLLNLTNRQL VVETKAGQLR RAPINPSVTT LTAHGGYMLN
     GKKYRDAPAP PPLQAPYRSV VNGSANSRGG ANTPRGGSRG GGRNGSPAHA NLPHRPAPQH
     QNHQPQQSHP QQQINGHHAP GGARGGRGGP AGTLPFRGGR GGGAPRAGFA TPQRGGAGFL
     PGNVGAGIPH PASAPPMYSA VPPPPSLDAP ARGSGRGRGR GGVARGGNRG GRGRGGVSRG
     SVPAAQAASQ PPQVAASASQ G
//
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