ID A0A3M7M1B6_9PLEO Unreviewed; 1412 AA.
AC A0A3M7M1B6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=5'-3' exoribonuclease 1 {ECO:0000256|PIRNR:PIRNR006743};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR006743};
GN ORFNames=GMOD_00004423 {ECO:0000313|EMBL:RMZ68214.1};
OS Pyrenophora seminiperda CCB06.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=1302712 {ECO:0000313|EMBL:RMZ68214.1, ECO:0000313|Proteomes:UP000265663};
RN [1] {ECO:0000313|EMBL:RMZ68214.1, ECO:0000313|Proteomes:UP000265663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB06 {ECO:0000313|EMBL:RMZ68214.1,
RC ECO:0000313|Proteomes:UP000265663};
RC TISSUE=Mycelium {ECO:0000313|EMBL:RMZ68214.1};
RX PubMed=24475219; DOI=10.1371/journal.pone.0087045;
RA Soliai M.M., Meyer S.E., Udall J.A., Elzinga D.E., Hermansen R.A.,
RA Bodily P.M., Hart A.A., Coleman C.E.;
RT "De novo Genome Assembly of the Fungal Plant Pathogen Pyrenophora
RT semeniperda.";
RL PLoS ONE 9:E87045-E87045(2014).
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; KE747814; RMZ68214.1; -; Genomic_DNA.
DR Proteomes; UP000265663; 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 Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR036867; R3H_dom_sf.
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:UP000265663};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR006743}.
FT DOMAIN 6..206
FT /note="Xrn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03159"
FT DOMAIN 254..654
FT /note="Xrn1 helical"
FT /evidence="ECO:0000259|Pfam:PF17846"
FT DOMAIN 702..890
FT /note="5'-3' exoribonuclease 1 D1"
FT /evidence="ECO:0000259|Pfam:PF18332"
FT DOMAIN 894..1117
FT /note="Exoribonuclease Xrn1 D2/D3"
FT /evidence="ECO:0000259|Pfam:PF18334"
FT DOMAIN 1135..1205
FT /note="5'-3' exoribonuclease 1 SH3-like"
FT /evidence="ECO:0000259|Pfam:PF18129"
FT REGION 423..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 158505 MW; A49F3F28B774058C CRC64;
MENRIPEFDC LYLDMNGIIH NCTHNDSDSV TARKSEDQMF ISIFNYIEHL FGKIKPKQLF
FMAIDGVAPR AKMNQQRARR FRTALDTEKA REKAIREGVE MPTEEAFDSN CITPGTAFMA
KLTQQLKYFI NKKVSEDIDW QGVEVVLSGH EVPGEGEHKV MEYIRQAKAQ PGYDPNRRHC
LYGLDADLIM LGLLSHDPHF SLLREEVTFG RQSQTKSKEL EHQNFYLMHL CIVREYLELE
FQELEEPGAL SFPFDMERVI DDFILMAFFV GNDFLPNLPH LHINEGALAL MFNVYKTVLP
KGKGYINEEG VINMERLAML LDELSNIEYR HFESENSDAA WFKDKSAKKE DVMKKTARRG
MVVMTTQQQA LFTSVKSWLN DYLAKKEQGP LDFPVSLPAE DRKFVQELAE KLHLPWKTVQ
NDDGDRHIQV TAPPKLVEGD SDDEDDTDDE SKKAIARIVQ KYEQAKVVDV SPEDAQSEMQ
KKYDQKFEAW KNDYYKSKFE WDRNNEEELR KLTENYVQGL QWVLYYYYRG VASWPWYYQY
HYSPMISDVK RGLKADINFK LGQPFKPFQQ LMGVLPDRSK SIVPKAYWPL MTNEDSPIID
FYPRDFTLDM NGKKQDWEAV VKIPFIQEDR LLKAMATKEQ DLTPDEKSRN SFGVSLKFTY
AKDLDFIYQS SLPGVFPDLP HCKCIENIFD LPTMDGLEYY IGLMDGAKLG ADALAGFPSL
KVLPFHGKLE FAGVNVFNQD SRNESMVITL LDTEPRQPVS HAKEKLGKAV HVGYPFLHEA
KVVKVSDELF DYFLSEDGVS APISVPHGPQ EISNWKKTAN RIETQYSKRL GINIGEIESL
VHVEMLKGLR KTDEGATIKE YGEVAGLQVD YATQAIVDEV VSEDQRFLEK EALPIEEEFP
VGARAFHLGD YAYGRPLQVV GHADNKATIM VAKLKKPEPN FGREVVRMAE RSTPYVPSYV
VARQLNMPPL ALSKLTSSFN VTSSGLKLNL GLNLKFEAKK LKVLGYSRKS PNGWEYSQKA
MELLAQYMIK FPEFVAAIIN NPTGDGWEDT DFYPPEIAKQ KVKEIGAWLK EVQTKSFEKV
PLDAEQLDSD TVKLIEQAAD ANFPLTQDME TKTVTKVPRV ALLKPSDAEQ RLGHQNFSIG
DRIVYVQDSG RVPIGSSGTV VGKTRTARVL LLDVVFDATF MSGTSLGDRC SPFRGSTVPA
TAVLNMSDQQ VVHYSSAAAA RRPQQTSQST YNMPRFGAPG GPQLIPAGTP PPLRGSYRGA
AGGINGRGGG MAPRQAPQQA QGQHTLPMHG GPPRGGRGGY APRGGQINGH ENHAPNGGNP
RGNLRGNSSD FVPRGRGDSF KRRGGGRGGF TIIDNTDPAE GVIPNNPNFQ PRNYSNVPPP
ATLDGGRGGR GRGRGRGRGR GDPRGGAPAA AQ
//
