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Database: UniProt
Entry: A0A8T0RE93_PANVG
LinkDB: A0A8T0RE93_PANVG
Original site: A0A8T0RE93_PANVG 
ID   A0A8T0RE93_PANVG        Unreviewed;       808 AA.
AC   A0A8T0RE93;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   RecName: Full=CBM20 domain-containing protein {ECO:0000259|PROSITE:PS51166};
GN   ORFNames=PVAP13_6KG167400 {ECO:0000313|EMBL:KAG2583380.1};
OS   Panicum virgatum (Blackwell switchgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Hiantes.
OX   NCBI_TaxID=38727 {ECO:0000313|EMBL:KAG2583380.1, ECO:0000313|Proteomes:UP000823388};
RN   [1] {ECO:0000313|EMBL:KAG2583380.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AP13 {ECO:0000313|EMBL:KAG2583380.1};
RA   Lovell J.T., Jenkins J., Shu S., Juenger T.E., Schmutz J.;
RT   "WGS assembly of Panicum virgatum.";
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in intercistronic processing of primary transcripts
CC       from chloroplast operons. The endonucleolytic activity of the enzyme
CC       depends on the number of phosphates at the 5' end, is inhibited by
CC       structured RNA, and preferentially cleaves A/U-rich sequences.
CC       {ECO:0000256|ARBA:ARBA00023436}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the RNase E/G family.
CC       {ECO:0000256|ARBA:ARBA00005522}.
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:KAG2583380.1}.
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DR   EMBL; CM029047; KAG2583380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8T0RE93; -.
DR   Proteomes; UP000823388; Chromosome 6K.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:TreeGrafter.
DR   FunFam; 2.60.40.10:FF:001568; Ribonuclease E/G-like protein, chloroplastic; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM20.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR004659; RNase_E/G.
DR   PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR   PANTHER; PTHR30001:SF1; RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000823388};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          94..204
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  89373 MW;  C9BDD33343645ED2 CRC64;
     MAARTLAPPS PLGSMWGPPR APAGSPVTEA SAAAAHAARR GGAAVSPALS GLRGRHSLCS
     VQFMDGLGSN IQAEVNLALS PKASMSNGND DSTITRKGFC TISWNLKADI QDGYLIFITG
     DPVTLGCWES NMAIQLAPSV ESNNIWTAEI KVPYGVHFKY NYFVREEKGS SSDIIWRPGP
     DYSLSIPSVG RKKQFIVVKD LWMKTSVAGL PAPSWGSWLM EAGSLEGEYF EGGNHWSIAE
     AHSARDTADQ DLSVDEETHD ASSSFPVENI TDNEEGMTLI PDAKIDIADS AEFEGISGYD
     EDKDDENDHM EDEYIEEILQ ADQSEISNDL KTLSSIQHAL RESNDDTNGS RWSQVRKGTK
     IMVQVVKEGL GTKGPTLSPF PCLRSRFWIL VSCGNKVGVS KKITGIERTR LKGITKLLRP
     PGFTLTARTV AAGHSWEDLQ RDLDGLLSTW KVITEHAQSA ALAAEEGVDG AVPVMLHRAK
     GQALSVVQDD FNEKVKRLVV DSPRTYHEVT SYLKEVAPEL CSRVDLYEKR KPIFDEYNIE
     KEIDNILCKR VPLNNGGSLV IEQTEALVSI DVNGGHSMFG QGTSQEKAIL EVNLEAAKQI
     ARELRLRDIG GIIVVDFIDM TDDLNKRLVY EEMKKAVEKD RSTVGVSELS KLGLMEITRK
     RVRPSVTFMI SEPCTCCHGT GRVEALDTSF SKIEREICRR LAASRRKSDP EKPKSWPRFV
     LRVDHEMCTY LTSGKKTKLG LLSSSLKVWI LLKIARGFSR GAFELLPYSE KENHEEKETE
     SESPQIEGSP KLHVFPIKKW MSRAKRAK
//
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