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Database: UniProt
Entry: K4A5C6_SETIT
LinkDB: K4A5C6_SETIT
Original site: K4A5C6_SETIT 
ID   K4A5C6_SETIT            Unreviewed;       989 AA.
AC   K4A5C6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=5'-3' exoribonuclease {ECO:0000256|PIRNR:PIRNR037239};
DE            EC=3.1.13.- {ECO:0000256|PIRNR:PIRNR037239};
GN   Name=101776459 {ECO:0000313|EnsemblPlants:KQK86694};
GN   ORFNames=SETIT_9G057500v2 {ECO:0000313|EMBL:RCV40482.1};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK86694, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EMBL:RCV40482.1, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK86694,
RC   ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC   {ECO:0000313|EMBL:RCV40482.1};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EMBL:RCV40482.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV40482.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK86694}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK86694};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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; AGNK02005326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM003536; RCV40482.1; -; Genomic_DNA.
DR   RefSeq; XP_004981452.1; XM_004981395.2.
DR   AlphaFoldDB; K4A5C6; -.
DR   STRING; 4555.K4A5C6; -.
DR   EnsemblPlants; KQK86694; KQK86694; SETIT_034080mg.
DR   GeneID; 101776459; -.
DR   Gramene; KQK86694; KQK86694; SETIT_034080mg.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_0_1; -.
DR   InParanoid; K4A5C6; -.
DR   OMA; AFLYQMC; -.
DR   OrthoDB; 167745at2759; -.
DR   Proteomes; UP000004995; Chromosome IX.
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   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:SF74; 5'-3' EXORIBONUCLEASE 4; 1.
DR   PANTHER; PTHR12341; 5'->3' EXORIBONUCLEASE; 1.
DR   Pfam; PF17846; XRN_M; 2.
DR   Pfam; PF03159; XRN_N; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          264..279
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          780..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..964
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  112731 MW;  3CC927B9EE4A9671 CRC64;
     MGVPAFYRWL ADRYPLTVSD AEEEEPVELE PGAFVPVDLR RPNPNGIEFD NLYLDMNGII
     HPCFHPEGRP APTTYDEVFK SIFDYIDHLF GLVRPRKLLY MAIDGVAPRA KMNQQRSRRF
     RAAKDAADAA AEEERLRKEF EAEGRTLAQK EKSEAIDSNV ITPGTQFMFV LSTALQYYIQ
     LRLNHTLGWQ SVKVILSDSN VPGEGEHKIM SYIRLQRNLP GFDPNTRHCL YGLDADLIML
     ALATHEVHFS ILREVISMPG QQEKCFLCGQ VGHLAAECRG PSQVDSAVEL PPIHKKKYQF
     LHIWVLREYL AKDLEIVDAP FKINFERLID DFVFMCFFVG NDFLPHMPTL EIREGAINLL
     MSIYRAEFIS MGGYLTDGGE VVLDRVEHFI QSVAFNEEQI FQKRARIQQA RENNEERNKI
     QRESTEENQY VDKVKLGEPG YRERYYAEKF KEEAESKPID QVRRDVVQKY VEGLCWVMRY
     YYQGVCSWQW FYPYHYAPFA SDLKDLAELE ITFFLGQPFK PFDQLMGTLP AASSNALPKY
     YGDLMTDPNS PLKSFYPKDF EIDMNGKRFA WQGVAKLPFI DETRLLAETR KLEDTLTEEE
     KFRNTTMFDI IYVRETHPLT AQIAFLYRMY NHLPRTDPYV IPIDPAASGG MNGFLCLSER
     NWYSITVTSP VKCFNGIAQN RVLNATYLNP QYHKHIPEPP VGVIVPGKIL KPSDFKPFPV
     LWHEDNSRRQ ARERPQVSGA LSGSLLGQAA HRLVKNSLQI KSGSAAGLLE MPYRGAPYGP
     GNRPRPAGPL GYERGFVDNP HHAHTSRSVP NSHPQFFGDA QANRQPMRIL ERPNSGSHEA
     GIHASMSKLT IHEGPRLHQN NRMQNSGYWP NQPHPNHYAG PPPQQPMQNI SFTPQRPFQT
     GGFPQQRPVN GVPPPLPPSN WIGKQPTGGP PGVPAKHDPR TAPDRQLKQD NPRSQQDKRQ
     QATKVYRVKT QATNGNGLSE SGKQEEPAA
//
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