PNP_BORT9
ID PNP_BORT9 Reviewed; 717 AA.
AC A1R0N0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
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=BT0805;
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135;
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=AAX18121.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000049; AAX18121.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041178593.1; NC_008710.1.
DR AlphaFoldDB; A1R0N0; -.
DR SMR; A1R0N0; -.
DR STRING; 314724.BT0805; -.
DR PRIDE; A1R0N0; -.
DR KEGG; btu:BT0805; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_12; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000001205; 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; 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_0000381869"
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 650..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..680
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; 80046 MW; 0897412A2B42DBB5 CRC64;
MRKILKLKVG REDLILETGL LAKQANGAVL ATYGGSTVLA TVCCSDSARE NLDFVPLSVE
YNEKYYAAGK IPGGFIKREG KPKDKEVLVS RLIDRPMRPL FDKRFGREIQ VVPTTLSTDQ
MNPPDIVGMN AAFAAVFLSD IPFNGPIAAV RIAYLNSEFI VNPSFDEIQD SILDIVVAGS
LDGITMVEGG ANEVSEEVLL AAIDQAYEYI KQICNLQKEF ILIVGEREKL PLAYEERVFE
FKAELKDFIY SELKDACFVK GKLNRDKAIK LVKQKAYEHF SSVSQVDEEN ETLFYKALDD
FEQEIVRRSI LENNLRTDGR NPTQIRDIVA EVDLLRRTHG SALFTRGETQ ALAVTTLGTS
IDEQIMDDID GDKRLNFMLH YNFPPFSVGE TGRLMTGRRE IGHGHLAQRS LEAMLPKKDD
FPYTIRVVSE ILESNGSSSM ATVCSGSMSL MAAGVPVKEQ VAGIAMGLVS EGDKYVILSD
ILGEEDHLGD MDFKVAGTKN GITGFQMDIK ISNVTKQLMK DALAQARIGR MHILSIMDSV
ISRSRDDISV NAPKIIQLQI DIDKISLVIG STGKTVKAIT DEFEVRVQIE QDGRITLFGT
DSLKMQKAKA RIESIVREPK IGEIYEGVVK KINSFGAFIE LTPTKEGFLS NRPKSRDDRY
GDMRHSRYGS GRHSRYGRDS RNTFAMRPPR LEEGQMVKVR ISDIDKFGKI ELELVRD
