ID A0A0K9PNR8_ZOSMR Unreviewed; 983 AA.
AC A0A0K9PNR8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ribonuclease E/G-like protein, chloroplastic {ECO:0000313|EMBL:KMZ70713.1};
GN ORFNames=ZOSMA_195G00090 {ECO:0000313|EMBL:KMZ70713.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ70713.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ70713.1}.
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DR EMBL; LFYR01000714; KMZ70713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PNR8; -.
DR STRING; 29655.A0A0K9PNR8; -.
DR OMA; VRDSWMR; -.
DR OrthoDB; 1206148at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; CBM_fam20.
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 NCBIfam; TIGR00757; RNaseEG; 1.
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; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 75..185
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 983 AA; 110334 MW; E9A9DB032689031E CRC64;
MELREACRPP LLVFGRNGGS GLRSAGIRRS KISLLPPPHF CYGMPVTKYF KTTQMHIINY
AHKSAASTLK GCSPIAFLGL CKVMWVIKAD VADGQILYIT GDPVALGCWN PEMAIPLSPS
NGHAHLWNAE IKVPFGIHFK YNYFIKEKDK PSNDVVWRPG PEFSISIPFP SKQSEYITVS
DLWLKKRIRN PVNSLWSSWI SDNDHSSKVL KMEDYQTSQT GEHTIQQSDR DHLIGEIFTN
YSLTDSGNSR VGKNININGI DSRKSFSERD QPVEEPWLFG SIFPCIVDSP IASDASDHPK
VAEVEVMEQE SNKKQCLVPA TEHQLVRIDE SVSTDILINS SVCTMQRIAI LENGKLVELL
LEPVKNNVQC DNVYLGVVTK LVPHMGGAFV DIGISRPSLM DIKQNREPFA YPPFKSKIKG
QKINGSIKIQ SEEHIDTEEH ELDVCVDENI DHDSLEADQH SSIHDVFDDH EVEDTIDISD
SQESVSSETD YDGSEVELDA EHEENDHPIE SKVTEDTRSS KVKWVHVRKG TKVIVQVVKE
GLGTKGPSLT ACPNLRSRFW ILISRCNRIG VSKKITGGER TRLRVIAKTL QPPGFGVTVR
TVAAGHSLEE LQKDLEGLLS TWKGIVEHAK SAALAADDGV EGAVPVILHR AMGQTLSVVQ
DYFNDKVKNM FVDSPRTYHE VSNYLQEIAP DLCNRVVLYK KSTPIFDDYG LEEEIDNILC
KRVLLSNGGS LVIEQTEALV SIDVNGGHSM LGQGTSQEKA VLDVNLAAAK QIARELRLRD
IGGIIVVDFI DMADESNKRL VYEEIKKAVE RDKSMVKVSE LSRHGLMEIT RKRVRPSVSF
LISEPCICCH GTGRVEALET SFSKIEREIL RMLATWNQKT DPENAKSWPR FVLKVDRYMC
NYLTSGKRTK LAILSSSLKV WILLKVARGF IRGEFEVKRF MDDKANNEDL VTISRLQSAE
ERSYIPNSKL TLFPIKKWKS RGR
//