PNP_BORHD
ID PNP_BORHD Reviewed; 717 AA.
AC B2S1E9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=BH0805;
OS Borrelia hermsii (strain HS1 / DAH).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 / DAH;
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX17302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000048; AAX17302.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043924534.1; NC_010673.1.
DR AlphaFoldDB; B2S1E9; -.
DR SMR; B2S1E9; -.
DR KEGG; bhr:BH0805; -.
DR HOGENOM; CLU_004217_2_2_12; -.
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; 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_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; 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; 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 PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; RNA-binding;
KW Transferase.
FT CHAIN 1..717
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000381868"
FT DOMAIN 553..612
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 622..715
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 659..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 717 AA; 80000 MW; 53C5FA6200CB29F7 CRC64;
MRKILRLKVG REDLILETGL LAKQANGAVL ATYGGSTVLA TVCCSDSVRE NLDFVPLSVE
YNEKYYAAGK IPGGFIKREG KPKDKEVLVS RLIDRPMRPL FDKRFGREIQ VVPTTLSTDQ
MNPPDIVGMN AAFAAVFLSD IPFNGPIAAV RLAYLNNEFI VNPSFDEIQD SILDIVVAGS
LDGITMVEGG ANEVSEEVLL SAIDKAYEYI KQICNLQKEF VSIIGEREKL PLAYEEGVFE
FKDELKNLIY SELKDACFVK GKLNRDKAIK LVKQKAYEHF SSISQVNEDN EFLFYKAFDD
FEREIVRKSI LENNLRTDGR TSTQIRDIVA EVDLLKRTHG SSLFTRGETQ ALAVTTLGTS
IDEQIMDDID GDKRLNFMLH YNFPPFSVGE TGRLMTGRRE VGHGHLAQRS LEAMLPKKDD
FPYTIRVVSE ILESNGSSSM ATVCSGSMSL MAAGVPVKEQ VAGIAMGLIS DGDKYVVLSD
ILGEEDHLGD MDFKVAGTKN GITGFQMDIK ISNVTKQLMK DALEQARIGR MHILSIMDSV
ISRSRDDISV NAPKIVQLQI DIDKISLVIG STGKTVKAIT DEFEVRVQIE QDGRITLFGT
DSLKMQKAKA KIESIVREPK IGEIYDGIVK KINSFGAFIE LTPIKEGFLS NRARSRDDRY
GDMRHSRYGS GRHSRYGRDN RNTFGMNPPR LEEGQIVKVK ISDIDKFGKI ELELVRD
