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Database: UniProt
Entry: F2I045_PELSM
LinkDB: F2I045_PELSM
Original site: F2I045_PELSM 
ID   F2I045_PELSM            Unreviewed;       695 AA.
AC   F2I045;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   OrderedLocusNames=SAR11G3_00337 {ECO:0000313|EMBL:AEA80812.1};
OS   Pelagibacter sp. (strain IMCC9063).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA80812.1, ECO:0000313|Proteomes:UP000009181};
RN   [1] {ECO:0000313|EMBL:AEA80812.1, ECO:0000313|Proteomes:UP000009181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA80812.1,
RC   ECO:0000313|Proteomes:UP000009181};
RX   PubMed=21515764; DOI=10.1128/JB.05033-11;
RA   Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT   "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT   3, isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3379-3380(2011).
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}.
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DR   EMBL; CP002511; AEA80812.1; -; Genomic_DNA.
DR   RefSeq; WP_013694977.1; NC_015380.1.
DR   AlphaFoldDB; F2I045; -.
DR   STRING; 1002672.SAR11G3_00337; -.
DR   KEGG; pel:SAR11G3_00337; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_5; -.
DR   OMA; DEMSPNA; -.
DR   OrthoDB; 9804305at2; -.
DR   Proteomes; UP000009181; Chromosome.
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; 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: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; 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   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:UP000009181};
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          619..686
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   BINDING         483
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   695 AA;  76154 MW;  DB55A74ED16E6B8E CRC64;
     MFNITKKEIT WGDKKLTLET GRVARQADGA VMLTCGETVI LATAVAAKQA KPDMDFFPLT
     VNYQEKYYAA GKIPGGYFKR EARPTEAETL ISRLIDRPIR PLFPSSFRNE TQVLPTVISY
     DKENDPEALA LIASSAALAI SGIPFMGPVA AAKVGMIDGE FVLNPTKEQI KDSQLELIVA
     GTEDAVLMVE SEASGLSEKQ MLDAVKFGHD KAKEVINLIK DFAKEAGKER WKIEEKDYSE
     LKEKISSAVA DDLQKAFDES DKQIRTGLIA AAKDKVTAMF EGDETYSKVE IGDQFKSVEK
     KIVRTQILKD SKRIDRRKLN EVRDIKCEVG VLPKVHGSSL FTRGETQALV VATLGTSDDE
     QRLETLDGAE RSRFMLHYNF PPYSVGEVGR IGTGRREIGH GKLAWRAINS SLPSKEEFPY
     TFRIVSEITE SNGSSSMATV CGASLALMDA GVPIKTPIAG IAMGLIKEGD DYSILSDILG
     DEDHLGDMDF KVAGTKDGIT SLQMDIKITG ITFDIMEKAL DQAKEGRIHI LGEMAKALTE
     SRKELSKNTP KMERIQVDKK DIAAVIGKGG ATIREIVELS GAKLDINDDG MVTIAAADEE
     SRMKAVQMVK DIVAKPEMGK IYKGKVVKIM EFGAFVNFLG KQDGLVHISQ LAAKRVENVS
     DVVKEGDEVS VKVVGFDRGK VKLSMKEVTE DTKSD
//
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