ID A0A0C7MTA0_9SACH Unreviewed; 1502 AA.
AC A0A0C7MTA0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=LALA0_S01e12596g {ECO:0000313|EMBL:CEP60511.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60511.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP60511.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60511.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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}.
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DR EMBL; LN736360; CEP60511.1; -; Genomic_DNA.
DR STRING; 1245769.A0A0C7MTA0; -.
DR HOGENOM; CLU_001581_1_2_1; -.
DR OrthoDB; 167745at2759; -.
DR Proteomes; UP000054304; 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 GO; GO:0006364; P:rRNA processing; 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; 3.30.1370.250; -; 1.
DR Gene3D; 3.40.50.12390; -; 2.
DR Gene3D; 6.10.140.950; -; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054304};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 1..227
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 271..681
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 722..915
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 919..1146
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1164..1234
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 1246..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 467..513
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1276..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 170603 MW; F656ACE3FB0BD5CC CRC64;
MGIPKFFRYI SERWPMISQL IDGSQIPEFD DLYLDMNSIL HTCTHANDDD VTKRLSEEEV
FAKIFAYIDH LFHTIGPKHT FYMAIDGVAP RAKMNQQRAR RFRTAMDAEK ALQKAIANGE
EIPKGEPFDS NCITPGTEFM AKLTQNLKYF IHDKVSNDSA WSSAKIILSG HEVPGEGEHK
IMEHIRRLRS QPDYNANTRH CIYGLDADLI MLGLSTHDPH FALLREEVTF GRRQKSQPLE
HQNFFLLHIS LLREYLELEF SEVADDLQFE YDFERILDDF ILVMFVIGND FLPNLPDLHL
NKGAFPVLLQ TFKEALKHVD GYINEQGTIN LSRFQVWLQY LGEFELMNFE KDDIDVEWFN
KQLENISLEG ERKRARLGKK LLLKQQKKIV GAIKPWLLKT SAAPFDASAM SSDEVPTFSL
DNDVIEDNLP FLKELAFDLG LFVAHSQSQD NYYLQLDVDG INPHETEEEH ANRVAALRKL
IKKYEQAVLV EDSEELEKEQ KLYAERFENW RDQYYKDKLD FSYHDEDKLR ELTENYVEGL
QWVLYYYYRG CPSWSWYYKY HYAPRISDVQ KGLNQIIKFG KGTPFRPFQQ LMAVLPERSK
NLIPVAYRPL MYDPKSPIGD FYPNEVELDK NGKTADWEAV VKLSFVDEKR LIDAMSTMED
KLTPEERNRN KFGSDLVFIY NPQIDDIYKS PLSGFFSDIE HNHCTEREYV PHSMDGLELL
YGLPSGAKLG AEALAGFPTL KTISFDSKLD YNGCMVFQQP SKQQSMLLTV KDAYNESNLT
LDEFAKTHLG KVVYTRWPNL RESKVLSITD GETIFELPKD SKQPQGKTSF TERKLDDVES
RFFNTQRAGL RRNYSVQKGV MLDEVRAIVR VVPVNGLTRT PDGAYVKTFS TVEEFYPMQL
VVEDVENKDQ RYMERTPVPV NEEFPEGLNV IFLGDYAYGG KAIVDGYSSN TRLKLTVEKH
TTDQEPTVGK VRAQLDQKLI HYYPSFIVSK KLQIHPLFLS RITSRFMVGG FGERPINFGL
EIKFESRHEK VLGYAKRNPK GWEYSDMTMA LLSEYKKNFP EFFFKLSTQA KDSPSFENMY
PGAKREDLKS VVDSVRAWLK SVKQNFVTVS FESDSLTKAS MIAVEDAIEK YAAAPAKISS
KQLAKVPREA ILDPQVSLAM LRTQKFDLGD RVIYIQDSGK VPLFSKGTVV GYTTIGPKLS
VQILFDSEIV AGNNFGGRLR TKRGLGLDSS FLLNLTNRQF IYHSKASKSV KEASKKPQKP
VKLAQTKPAA AATRQQDEAT KKKQAHELLS HIKGAEAETQ TAQVKGAAQD TNVQDKNKSY
TGDEAEVNSP NDRIIASNIY NAVFNQFADA SPVPGPNPFP QRLPYEAGPP NAVPPHLIGR
VPPPPPHMGF YPSQGPVLPM GPPPAGHFVH PYQMSANAQD VNGNFAGEGK SENQNDGLSE
TKNGLYHGNA DRKSGHASFG GRENASRGGS RGRGDFRGRG RGRGRGRGRG RGRGRGNSSP
SS
//
