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
//