ID A0A2J6L5T3_LACSA Unreviewed; 1068 AA.
AC A0A2J6L5T3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN ORFNames=LSAT_2X8340 {ECO:0000313|EMBL:PLY82688.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY82688.1};
RN [1] {ECO:0000313|EMBL:PLY82688.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Acts as an
CC endogenous post-transcriptional gene silencing (PTGS) suppressor.
CC {ECO:0000256|PIRNR:PIRNR037239}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC ECO:0000256|PIRNR:PIRNR037239}.
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:PLY82688.1}.
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DR EMBL; NBSK01005001; PLY82688.1; -; Genomic_DNA.
DR STRING; 4236.A0A2J6L5T3; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_2X8340_mrna; cds-PLY82688.1; gene-LSAT_2X8340.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_2X8340_mrna; cds-PLY82688.1; gene-LSAT_2X8340.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
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; 3.40.50.12390; -; 2.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR004859; Xrn1_N.
DR InterPro; IPR017151; Xrn2/3/4.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12341:SF41; 5'-3' EXORIBONUCLEASE 1; 1.
DR PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR037239};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037239};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR037239};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR037239};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 263..278
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1028
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 120954 MW; 7EA6D313C14D41EA CRC64;
MGVPAFYRWL AEKYPMVVVD VIEEEPVVIG GVKIPVDTSK PNPNKIEYDN MYLDMNGIIH
PCFHPEDRPS PTSFSEVFQC VFDYIDRLFV MVRPRKLLYM AIDGVAPRAK MNQQRSRRFR
AAKDAAEAAA EEERLREEFE KEGRTLPPKQ ESQTFDSNVI TPGTEFMAVL SIALQYYVHK
RLNNDPGWKS IKVILSDANV PGEGEHKIMS YIRLQRNLPS FDPNTRHCLY GLDADLIMLA
LATHEVHFSI LREVVFIKGE QGKCFVCGQS GHMAAGCKGK VKRKAGEFDE KGGTEEPKKP
YQFLNIWTLR EYLKHEMQIP NVEIDLERII DDFVFLCFFV GNDFLPHMPT LDIREGAINL
LFAVYKKEFK AMGGYLTDAS KPDLVKVEHF IQAVGSFEEA IFQKRARMLQ KQLERVKRDK
AQAKRGDDGQ PRVDPDSLVP ITRFDGARLA CGPSPSPYKQ KRSRKGVKKN EQQVKLATKD
LSALELDIQH KRPMQCDDEK IDIRAKKVAR LSSGNTVGAA IVEAETSHER EAFENKEELK
VRLKGVLREK SDAFNSEELE DKIKLGAPGW KERYYEEKFS ATTIEEMDAI RRDVVLKYTE
GLCWVMHYYY EGVCSWQWFY PYHYAPFASD LKDLNKLNIK FELGSPFKPF NQLLGVFPAA
SAHALPEQYR KLMTDPNSPI VDFYPTDFEV DMNGKRFAWQ GIAKLPFIDE TRLLEEVKKV
EHTLTNEETQ RNSRMCDMLF VSISHKLSPY IFSLDDQTIK YGSKKRAQIN QQIKPESSDG
MNGYLSLPSG DPCPKVFRSP IEGLEDIKDN RVICAIYKLP DPHPHIPRPP PGVKLPKKTV
TKDDLTETPA LWHEDSGPKH WENRRIHTRT RPDLFPGSGW LWRLTDLWST AYKPXAAAPP
PFQQTGPHNH AAQTNRHHPS GNDSGEPWSG QPQGGGRRRN RRNRYRSAGG GGSHQDSGSN
IEGKLSGGMN QNQNPVRMWV PRAGQSGGGA TTKPPPNKGE KFTKLPPPPP LPPQQPPQPP
PAHECNKVIS NPPPPSVGSK KVKKRGKKVY KAANTATAAT TSTTTMSS
//
