PNP_BIFLO
ID PNP_BIFLO Reviewed; 913 AA.
AC Q8G447;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=BL1546;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25338.1; -; Genomic_DNA.
DR RefSeq; NP_696702.1; NC_004307.2.
DR RefSeq; WP_010081538.1; NC_004307.2.
DR AlphaFoldDB; Q8G447; -.
DR SMR; Q8G447; -.
DR STRING; 206672.BL1546; -.
DR PRIDE; Q8G447; -.
DR EnsemblBacteria; AAN25338; AAN25338; BL1546.
DR KEGG; blo:BL1546; -.
DR PATRIC; fig|206672.9.peg.1600; -.
DR HOGENOM; CLU_004217_1_0_11; -.
DR OMA; LHILDVM; -.
DR PhylomeDB; Q8G447; -.
DR Proteomes; UP000000439; 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..913
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329532"
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..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..913
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 913 AA; 101847 MW; 44BF8295382F2AFB CRC64;
MEGPEIKAVE AVIDNGSFGK RTLRFETGRL AQQADGAVAA YLDDDSMILS TTTAGSSPKE
NYDFFPLTVD VEEKMYAAGK IPGSFFRREG RPSSEAILAC RIIDRPLRPL FPHTLRNEVQ
VVETVLAVNP DDAYDVIALN AASASTMISG LPFEGPVSGV RLALIDGQWV AFPRWSERER
AVFEIVVAGR VIENGDVAIA MIEAGAGKNA WHLIYDEGQT KPDEEVVAGG LEAAKPFIKV
ICEAQDELKK IAAKETKEFQ LFPEYTDELY ARIDEIAHKD LDEALSIAEK LPRQDRIHEI
KEHVREVLAD EFTDMDDAEK DKELGNAFKE LQRQIVRRRI LTEDYRIDGR GLRDIRTLSA
EVDIVPRVHG SALFQRGETQ ILGVTTLNML KMEQQIDALS GPQSKRYMHN YEMPPYSTGE
TGRVGSPKRR EIGHGALAEK ALVPVLPSRE EFPYAIRQVS EAIGSNGSTS MGSVCASTLS
LLAAGVPLKA PVAGIAMGLV SGDVDGKHIF KTLTDILGAE DAFGDMDFKV AGTSEFITAL
QLDTKLDGIP ADILAAALQQ AKEARATILE VINECIDGPA EMSEFAPRII TTSVPVEKIG
EVIGPKGKMI NQIQEDTGAE IAIEDDGTVF ISSEGGEAAE KAKAIIDQIA NPHVPEAGET
YNGKVVKTTS FGAFVNLTPG TDGLLHISQI RNLANGERID AVEDVLKEGD TVEVIVQGVD
DRGKISLAIP GFEDQENNAR PSRGDRDDRR GGRGRGDRDD RRGGRGRRSE RDDRDFDDRD
DRPRRRRSDD FEDDYDDRPR RRRSDDRDFD RDDRDDDRPR RRRSADRDFD DRDDRDARDS
RDDDRPRRRR SSDRDDRGDR DDRRGGSRGR GRGSDRNPRY ATDDNYDDYR ADREERTERP
RRRVRRDFDP FED
