ID B9D358_CAMRE Unreviewed; 735 AA.
AC B9D358;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 82.
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 ECO:0000313|EMBL:EEF13588.1};
GN ORFNames=CAMRE0001_1493 {ECO:0000313|EMBL:EEF13588.1};
OS Campylobacter rectus RM3267.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF13588.1, ECO:0000313|Proteomes:UP000003082};
RN [1] {ECO:0000313|EMBL:EEF13588.1, ECO:0000313|Proteomes:UP000003082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM3267 {ECO:0000313|EMBL:EEF13588.1,
RC ECO:0000313|Proteomes:UP000003082};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (AUG-2008) 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: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:EEF13588.1}.
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DR EMBL; ACFU01000017; EEF13588.1; -; Genomic_DNA.
DR RefSeq; WP_004320079.1; NZ_ACFU01000017.1.
DR AlphaFoldDB; B9D358; -.
DR STRING; 553218.CAMRE0001_1493; -.
DR eggNOG; COG1185; Bacteria.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000003082; 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; cd11364; RNase_PH_PNPase_2; 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 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|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};
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 675..734
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 651..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 735 AA; 79701 MW; 9FD6F2E5FC551FB9 CRC64;
MQYSIEVNNQ VEIYDINKVA KQASGAALLR VKNTVVLATV AREDTQVSED FLPLTVQYIE
KTYAAGRIPG GYVKRETKPG DFETLTSRII DRSLRPLFPK GYAYPTQIVV MVLSCDPEVD
LQVVALNAAS VALYLSDIPV NAPVCGVRVG YIDNKFVINP SNSELKTSAL DLYVAGVKDE
LLMIEMRSIA TQKDEMMPIA LDPMMDPNLG GEVIATQDMN EFSEDLIVEA IAEAGKAILR
ASNAYEEAFS QHKKEDAQLE LKPEIENESI AVYLDEFYKN EVKAAINQMA KSERAGELNK
IAKQILTDEV AQKEGWEEEV VSNVLAKFKK KIVREQIINE GVRADGRGLK DVRPISIETN
ILPNAHGSCL FTRGQTQALV VATLGTDGDA QMYDMLTEKG AVTDKFMFNY NFPGFSVGEA
SPLKAPGRRE LGHGNLAKRA LAPSIDSDSP YTIRLVSEIL ESNGSSSMAS VCGGSLALRA
AGVDTPKLVA GVAMGLIFEG EKHAVLTDIM GLEDHDGDMD FKVAGSKDGI TALQMDIKLG
GISLDVLKEA LLQACEGRLH ILNLMETANK NISVNEEILP KLELFSVDPG KIVDIIGQAG
KTIKEIIEKF DVAIDLDREK GEVKIAGAQK SSVDAAKDYI IQIVSKDGGK GFGGRRGGRD
GKEGRAHKTP EFNIGDEFEG EVKSVVEFGA FIGLPGGVDG LLHISKIKTP LKAGDRVKVK
ISEQKGHKIS LSLAQ
//
