PNP_BIFAA
ID PNP_BIFAA Reviewed; 892 AA.
AC A1A008;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=BAD_0260;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-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; AP009256; BAF39041.1; -; Genomic_DNA.
DR RefSeq; WP_003807809.1; NC_008618.1.
DR AlphaFoldDB; A1A008; -.
DR SMR; A1A008; -.
DR STRING; 1680.BADO_0268; -.
DR PRIDE; A1A008; -.
DR EnsemblBacteria; BAF39041; BAF39041; BAD_0260.
DR KEGG; bad:BAD_0260; -.
DR HOGENOM; CLU_004217_2_2_11; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000008702; 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 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; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR014069; GPSI/PNP.
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; PF00575; S1; 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 TIGRFAMs; TIGR02696; pppGpp_PNP; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..892
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329531"
FT DOMAIN 587..646
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 658..730
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 407..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 892 AA; 99740 MW; 046446FECA427721 CRC64;
MEGPEIKAVE AVIDNGSFGK RTLRFETGRL AQQADGAVAA YLDDDSMILS TTTAGSSPKE
NYDFFPLTVD VEEKMYAAGK IPGSFFRREG RPSSEAILAC RIIDRPLRPL FPHTLRNEVQ
VVETVLAVNP DDAYDVVALN AASASTMISG LPFEGPVSGV RLALIDGQWV AFPRWSERER
AVFEIVVAGR VVENGDVAIA MIEAGAGKNA WHLIYDEGQT KPDEEVVAGG LEAAKPFIKV
ICEAQAELKK IAAKETKEFQ LFPEYTEDLY NRIDEIAHAD LDEALSIAEK LPRQDRIHEI
KEGVKATLAG EFTDMEDAEK DKEIGNAFKE LQRQIVRRRI LTQDYRIDGR GLRDIRTLSA
EVDIVPRVHG SALFQRGETQ ILGVTTLNML KMEQQIDALS GPQSKRYMHN YEMPPYSTGE
TGRVGSPKRR EIGHGALAEK ALVPVLPSRE EFPYAIRQVS EAIGSNGSTS MGSVCASTLS
LLAAGVPLKA PVAGIAMGLV SGDVDGQHIY KTLTDILGAE DAFGDMDFKV AGTSEFITAL
QLDTKLDGIP ADILASALQQ AKEARTTILE VINECIDGPA EMSPYAPRII TTTVPVDKIG
EVIGPKGKMI NQIQEDTGAE IAIEDDGTVY ISSEGGEAAE KAKEIIDQIA NPHVPEAGET
YNGKVVKTTS FGAFVNLTPG TDGLLHISQI RNLANGERID AVEDVLKEGD TVEVVVQGVD
DRGKISLAIP GFEDQESSAP RRDRGDRDDR RGGRGRRDDR RRSDDRDDRD YDDRPRRRRS
DRDDDRDYDD RPRRRRSDRD DRDYDRDDRR SSRSDRDDRD YDDRPRRRRS DRDDRDYDRD
DRRSDRRRGS RRDDRNPRYA ADENYDEYRA DREERSERPR RRVRRDFDPF ED
