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Database: UniProt
Entry: K5YZP5_9PROT
LinkDB: K5YZP5_9PROT
Original site: K5YZP5_9PROT 
ID   K5YZP5_9PROT            Unreviewed;       716 AA.
AC   K5YZP5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595};
DE            EC=2.7.7.8 {ECO:0000256|HAMAP-Rule:MF_01595};
DE   AltName: Full=Polynucleotide phosphorylase {ECO:0000256|HAMAP-Rule:MF_01595};
DE            Short=PNPase {ECO:0000256|HAMAP-Rule:MF_01595};
GN   Name=pnp {ECO:0000256|HAMAP-Rule:MF_01595};
GN   ORFNames=MXAZACID_05366 {ECO:0000313|EMBL:EKN00424.1};
OS   Acidocella sp. MX-AZ02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKN00424.1, ECO:0000313|Proteomes:UP000006217};
RN   [1] {ECO:0000313|EMBL:EKN00424.1, ECO:0000313|Proteomes:UP000006217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKN00424.1,
RC   ECO:0000313|Proteomes:UP000006217};
RX   PubMed=23405365;
RA   Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT   "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT   AZ02.";
RL   Genome Announc. 1:E00041-12(2013).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC       single-stranded polyribonucleotides processively in the 3'- to 5'-
CC       direction. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC       Rule:MF_01595}.
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:EKN00424.1}.
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DR   EMBL; AMPS01000062; EKN00424.1; -; Genomic_DNA.
DR   RefSeq; WP_008493131.1; NZ_JH976207.1.
DR   AlphaFoldDB; K5YZP5; -.
DR   STRING; 1214225.MXAZACID_05366; -.
DR   PATRIC; fig|1214225.3.peg.1038; -.
DR   HOGENOM; CLU_004217_2_2_5; -.
DR   Proteomes; UP000006217; Unassembled WGS sequence.
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   CDD; cd02393; KH-I_PNPase; 1.
DR   CDD; cd11363; RNase_PH_PNPase_1; 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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
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:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01595};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01595}.
FT   DOMAIN          622..690
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   BINDING         486
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         492
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   716 AA;  76586 MW;  E6FF641501FD76E6 CRC64;
     MFDKFFRKEM EWGGKTLILE TGKVARQADG AVVASYGDTV VLATVVGAKS AKPGQDFFPL
     TVNYQEKFYA AGRIPGGFFK REGRPTEKET LVSRLIDRPI RPLFPEGFRN EVQVVVNVLS
     HDLDNDPDVV GLVAASAALT LSGIPFFGPV GAARVGYING AYVLNPTTSE REESKLDLVL
     AGTTEGVLMV ESEASELSEE VMLGAVTFGH QSFQPVIQAI IELAESAAKE PWDLPEESEE
     TKTLKARVDA LARAAITEAY KETQKQVRYE KLAAAKKEAA AKLTEEGLNA EAAKGLFKAL
     EADIVRNAIL DTGLRIDGRD TKTVRPILSE VGVLPRTHGS ALFTRGETQA LVVATLGTAQ
     DEQVVDAIEG EFKEHFMLHY NFPPFSVGET GRMGSPGRRE IGHGKLAWRA VHPLLPTKEA
     FPYTLRVVSE ITESNGSSSM ATVCGTSLSL MDAGVPLKSP VAGIAMGLIK EDKGFAVLSD
     ILGDEDHLGD MDFKVAGTEE GITALQMDIK ITSITPEIMK IALEQAKGGR LHILGEMAKA
     ITGNRDGVSA NAPKIVTTSV PKDKIRDVIG TGGKVIRDIV EKTGAKVDIG DDGTVKIAAS
     DDKKIQAALD MIKGIVAEPE VGVIYNGKVV KTADFGAFVN FLGAKDGLVH ISELAQGRVA
     KTTDVVKQGD AVKVKVIGFD DRGKVKLSMR VVDQETGADI SDQVGSTKGK REQAEG
//
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