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Database: UniProt
Entry: A0A1D6MQ10_MAIZE
LinkDB: A0A1D6MQ10_MAIZE
Original site: A0A1D6MQ10_MAIZE 
ID   A0A1D6MQ10_MAIZE        Unreviewed;       767 AA.
AC   A0A1D6MQ10;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   03-MAY-2023, entry version 36.
DE   RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN   ORFNames=ZEAMMB73_Zm00001d040311 {ECO:0000313|EMBL:ONM31120.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM31120.1};
RN   [1] {ECO:0000313|EMBL:ONM31120.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM31120.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Acts as an
CC       endogenous post-transcriptional gene silencing (PTGS) suppressor.
CC       {ECO:0000256|PIRNR:PIRNR037239}.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006994,
CC       ECO:0000256|PIRNR:PIRNR037239}.
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DR   EMBL; CM007649; ONM31108.1; -; Genomic_DNA.
DR   EMBL; CM007649; ONM31120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6MQ10; -.
DR   ExpressionAtlas; A0A1D6MQ10; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
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:SF56; 5'-3' EXORIBONUCLEASE; 1.
DR   PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR   Pfam; PF17846; XRN_M; 1.
DR   Pfam; PF03159; XRN_N; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR   SMART; SM00343; ZnF_C2HC; 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   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          263..277
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          452..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  88521 MW;  7976B5EED1A6DD05 CRC64;
     MGVPAFYRWL AEKYPMVVVD VVEEEPVEIE GVKVPVDTSK PNPNSLEFDN LYLDMNGIIH
     PCFHPEDRPS PTTFGEVFQC MFDYIDRLFV MVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
     AAKDAADAAA EEERLREEFE REGRKLPPKQ QSQTCDSNVI TPGTEFMAVL SVALQYYIHR
     RLNYDPGWKQ IKVILSDANV PGEGEHKIMS YIRGQRNLSG FNPNTRHCLY GLDADLIMLA
     LATHEVHFSI LREVVYTPGQ QDKCFLCGQV GHLAANCEGK VKRKAGEFDE KGGAIVPKKP
     YQFLNIWTLR EYLEYEFRMP NPPFKIDFER IVDDFIFMCF FVGNDFLPHM PTLEIREGAI
     NLLMAVYKKE FPSMGGYLTD SCTPDLSRVE HFIQAVGSYE DKIFQKRARL HQRQAERIKR
     EKAQAKRGDD LDPHVRDDLI VPIQRFQGSR LASGAVPVPY EQNGSHKDNK ERNSRARKAA
     RVSTSGSSIA SALVEAENDL EAQECENKEE LKSMLKDALR EKSDIFNSDN PEEDKVKLGE
     PGWRERYYEE KFGARTPEQI EEIRRDVVLK YTEGLCWVMH YYYEGVCSWQ WFYPYHYAPF
     ASDLSGLGQL NIKFELGTPF KPFDQLMGVF PAASAHALPL QYRRLMTDPN SPIIDFYPTD
     FEVDMNGKRY SWQGIAKLPF IDEDRLLAEI KKVEHTLTPE EARRNSIMCD MLFVNGSHPL
     SPYIYSLNSK FGHLPDKRRN EIKEKLDPSA RLTKLNIVVV RQVILFC
//
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