ID B9SI65_RICCO Unreviewed; 948 AA.
AC B9SI65;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE AltName: Full=Polynucleotide phosphorylase 1 {ECO:0000256|ARBA:ARBA00031451};
GN ORFNames=RCOM_1321070 {ECO:0000313|EMBL:EEF36667.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; EQ973969; EEF36667.1; -; Genomic_DNA.
DR RefSeq; XP_002525684.1; XM_002525638.2.
DR AlphaFoldDB; B9SI65; -.
DR STRING; 3988.B9SI65; -.
DR GeneID; 8286492; -.
DR KEGG; rcu:8286492; -.
DR eggNOG; KOG1067; Eukaryota.
DR InParanoid; B9SI65; -.
DR OrthoDB; 937144at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR CDD; cd04472; S1_PNPase; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01595; PNPase; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF17; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 2.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EEF36667.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF36667.1}.
FT DOMAIN 765..834
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 837..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 102792 MW; ED850120A022C6AA CRC64;
MLANPSTSSL HTIPYHPQTS PSFSNSITTR CKLFLSPNCP RFIHSSFSKF PSLSLLLPCK
RGERFSARAL EDPEITESVI VDGPQFFPQA VSVKIPFGDR HILVETGHTG RQASGSVMVT
DGETIVYTTV CLDDVPSEPS DFFPLSVNYQ ERFSAAGRTS GGFFKREGRA KDHEVLICRL
IDRPLRPTML KGFYHETQIL SWVLSYDGLH SSDALAVTAA GIAVALSEVP TTKAIAGVRV
GLVGDKFIVN PTTKEMEESK LDLVMAGTDS AILMIEGYCN FLPEEKLLEA VQVGQDAVRA
ICNEVDALVK KCGKPKMHDA IKLPPPELYK HVKEIAGDEL VNVLQIRNKI PRRKALSSLE
EKVISILTEE GFVSKDTSFG TTETVADLLE EEEEDEEFVV DGEVDEGDIH IKPVSRKSSP
LLYSEVDVKL VFKEVTSQFL RRRIVEGGKR SDGRNADGIR PINSRCGLLP RAHGSALFTR
GETQSLAVAT LGDKQMAQKV DNLVDVDEFK RFYLQYSFPP SSVGEVGRMG APSRREIGHG
MLAERALEPI LPSEADFPYT IRVESTITES NGSSSMASVC GGCLALQDAG VPVKCSIAGI
AMGMVLDTEE FGGDGTPLIL SDITGSEDAS GDMDFKVAGN EDGVTAFQMD IKVGGITLPV
MRRALLQARD GRKHILAEML KCSPSPSKRL SKHAPLIHMM KVDPQKVNMI IGSGGKKVRS
IIEETGVEAI DTDDDGTIKI TAKDLSSLEK SKSIISNLTM VPTVGDIYRN CEIKTIAPYG
VFVEIAPGRE GLCHISELTS SWLAKAEDAF KVGDRVDVKL IEVNEKGQLK LSRKALLPEP
TVENPDGKTT DKDYPKGTVN SSKVGITEAK IEQLKGDTSS PEVATSPKSN AVENTPVPQK
KIYKRTISST KNGPNTNKDR PKKGGNKVVS GIAASDGNTL VNGEAKIG
//
