ID   PNP_SPICI               Reviewed;         702 AA.
AC   Q14LB9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE   AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN   Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; ORFNames=SPICI19_061;
OS   Spiroplasma citri.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=2133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GII-3-3X;
RA   Carle P., Saillard C., Blanchard A., Carrere N., Carrere S., Duret S.,
RA   Eveillard S., Gaurivaud P., Gourgues G., Gouzy J., Henry A., Salar P.,
RA   Laigret F., Bove J.M., Renaudin J., Foissac X.;
RT   "The partial chromosome sequence of Spiroplasma citri GII3-3X.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC       single-stranded polyribonucleotides processively in the 3'- to 5'-
CC       direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC         EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR   EMBL; AM285320; CAK99711.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q14LB9; -.
DR   SMR; Q14LB9; -.
DR   STRING; 2133.SCITRI_001688; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   Gene3D; 3.30.230.70; -; 2.
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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR11252; PTHR11252; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF03726; PNPase; 1.
DR   Pfam; PF01138; RNase_PH; 2.
DR   Pfam; PF03725; RNase_PH_C; 2.
DR   Pfam; PF00575; S1; 1.
DR   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF46915; SSF46915; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   SUPFAM; SSF55666; SSF55666; 2.
DR   TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
FT   CHAIN           1..702
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000329861"
FT   DOMAIN          558..618
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          628..696
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   702 AA;  77164 MW;  15E38C9BD7FEE5FB CRC64;
     MAKQVFKKII NNQELIVEHG QLAKQASGSV LVRYGDTVVL VTATVNNKLS EVDFFPLTVV
     FQEKLYSVGK IPGGFLKREG KPSEYGTLSA RVIDRALRPL FSENFRNEVQ IVINVLAVDN
     DNDVRMVSLF AASLALSISK IPFAGPVAGA LVTVDQKNNI IINPTLEQIN DGQMELIVAG
     TDEAINMVEA GAKEVSENLM LQAILAGHDV IQQLIAFQHE IIAKVGVPKM EVELFQVRPE
     IITYVNNNYA KDLITAARIK EKTKRYETIE HLIEQAIKNY PMPVSLSEKE QKQLTVELKT
     ALHNIIRQEV RRQILIDKTR LDGRKLDQIR PLSSEIDILP VVHGSALFTR GETQVLSVVT
     LGALGENQII DGITDEESKR FMHHYNFPAF SVGETGRMGP PSRREIGHGA LGEKVLLQII
     PSEKVFPYTI RIVSEVLESN GSTSQASICA ATLALMAAGV PITAPVVGIA MGLIKEKNNY
     TILTDIQGME DHLGDMDFKV AGTATGICAL QMDIKIVGIN KAILQEALKA AKKARLTILD
     NVLATISAPR THLAPTAPKM KTFMIPVDKI REVIGPGGKM ITAIIEKSDD VKIDIEDDGQ
     VTIYHKETTA IEKAYQLIKA IAMPVVVGEK IIGPVVKIEK FGVFVHLKEN LDGLIHISKL
     AKQHVEKAED IVQLNDIVKV KVIEIDGKGK IKLQLIEILP KK