ID G7KE17_MEDTR Unreviewed; 1006 AA.
AC G7KE17; A0A0C3XNC1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative ribonuclease E {ECO:0000313|EMBL:RHN56422.1};
DE EC=3.1.26.12 {ECO:0000313|EMBL:RHN56422.1};
DE SubName: Full=Ribonuclease E/G family protein {ECO:0000313|EMBL:AES98508.2};
GN Name=11409378 {ECO:0000313|EnsemblPlants:AES98508};
GN OrderedLocusNames=MTR_5g069430 {ECO:0000313|EMBL:AES98508.2};
GN ORFNames=MtrunA17_Chr5g0429311 {ECO:0000313|EMBL:RHN56422.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES98508.2, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES98508.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES98508.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES98508,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AES98508.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES98508,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:AES98508}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES98508};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN56422.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN56422.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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}.
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DR EMBL; CM001221; AES98508.2; -; Genomic_DNA.
DR EMBL; PSQE01000005; RHN56422.1; -; Genomic_DNA.
DR RefSeq; XP_003615550.2; XM_003615502.2.
DR AlphaFoldDB; G7KE17; -.
DR STRING; 3880.G7KE17; -.
DR PaxDb; 3880-AES98508; -.
DR EnsemblPlants; AES98508; AES98508; MTR_5g069430.
DR GeneID; 11409378; -.
DR Gramene; AES98508; AES98508; MTR_5g069430.
DR KEGG; mtr:11409378; -.
DR eggNOG; ENOG502QPXM; Eukaryota.
DR HOGENOM; CLU_003468_5_3_1; -.
DR OrthoDB; 1206148at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR Proteomes; UP000265566; Chromosome 5.
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 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; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RHN56422.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 72..181
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 1006 AA; 113336 MW; 0FF3620B58C0EB58 CRC64;
MLMEFIAEVG FLHHPHHLFT PFSNPYTLSP KRHIFHHAPL HGEYRFMCCL KNHKSVRRLA
SFTTTQKGNS TTSVDDLCKI IWTVEADLED GHLLYITGDP AVLGCWKPNM AVLMSPTEHT
NIWKAESQIA FGLNFKYNYF IKEKSRSSSD IIWKPGPAFS LSVPLTALAD NEIVVRDLWI
RSNFHISSAH AWNPCTEETY LLKQPSIFFP VKDERRNMSL LENDFLKTET LILEDQLFFD
SEDMAILSNK DSHPINVLSE NYQPVEEPWL LHSLRSVISE DKTESNESKT NDIVKEQVKL
VDSEELLPEE SSNAILKDPV STIILINSSM KSVDSEELLP EESSNTILKD PVSTIILINS
SICTMQRIAV LEDEKLVELL LEPVKTNVQS DSVYVGEITK LVPSMGGALV DIGNSRPSLM
DIKPYKEPFI FPPFRRRTKK QEIVLKGKND HMSRATDIPG GIRDIHSEDD CLKSVHNDYD
EHETDDDFCL SEVLKENVNG SVVDDEVEAD FEDDVEGADV HTEGKMNNGS LSLGMNGSIN
FHILPTKDTK REMGENKWIQ VRSGTKIVVQ VVKEGLGTKG PTLTAFPILR SRFWVLTTRC
DKIGVSKKIS GAERTRLKVI AKTLQPEGFG LTVRTVAAGH SFEELQKDLE GLLSTWKNIM
ENAKSSALAA DERVEGAVPA ILHRAMGQTL SVVQDYFNEN VKKMVVDSPR TFHEVTNYLQ
DIAPDLCDRV ELYNKKVPLF DEYNIEGELD NILSKRVPLA NGGSLIIEQT EALVSIDVNG
GHGMLDHDTS KEKAILDVNL AAAKQIAREL RLRDIGGIIV VDFIDMTDEA NKRLVYEEVK
KAIERDRSVV KVSELSRHGL MEITRKRVRP SVTFMVSEPC DCCHATGRVE ALETSFFKIE
QQICRILATM NHKGEPQKPK SWPKFILRVD HHMCTYLTSG KKTKLGILSS SLKVWILLKV
SRGFTRGTFE IKPYTDDKVG RNQHQVAVSK AKPKSTFVRV IKSKAG
//
