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PNP_BORRA
ID   PNP_BORRA               Reviewed;         717 AA.
AC   B5RQE3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BRE_816;
OS   Borrelia recurrentis (strain A1).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000993; ACH95027.1; -; Genomic_DNA.
DR   RefSeq; WP_012539180.1; NC_011244.1.
DR   AlphaFoldDB; B5RQE3; -.
DR   SMR; B5RQE3; -.
DR   EnsemblBacteria; ACH95027; ACH95027; BRE_816.
DR   KEGG; bre:BRE_816; -.
DR   HOGENOM; CLU_004217_2_2_12; -.
DR   OMA; LHILDVM; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000000612; 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; 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; 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; 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   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_1000147892"
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..678
FT                   /note="Disordered"
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;  80352 MW;  7EF498B499B96728 CRC64;
     MRKILKLKIG REDLILETGL LAKQANGAVL ATYGGSTVLA TVCCSDSIRE NLDFVPLSVE
     YNEKYYAAGK IPGGFIKREG KPKDKEVLVS RLIDRPMRPL FDKRFGREIQ VVPTTLSTDQ
     MNPPDIVGMN AAFTAVFLSD IPFNGPIAAV RIAYLNDEFI VNPSFDEIQD SVLDIVVAGS
     LDGITMVEGG ANEVSEEILL DAIDKAYTYI KQICDLQKEF IYLIGEREKL PLAYEEKVFE
     FKDDLRSLIY FELKDACFVR GKLNRDKAIK LVKQKAYEHF SSLEQLNDEN EILFYKACDD
     FEQEIVRKSI LEDNLRTDGR TPTQIRDIIA EVDLLKRTHG SALFTRGETQ ALAVTTLGTS
     IDEQVMDDID GDKRLNFMLH YNFPPFSVGE TGRLMTGRRE IGHGHLAQRS LEAMLPKKDD
     FPYTIRVVSE VLESNGSSSM ATVCSGSMSL MAAGVPVKEQ VAGIAMGLIS NDDKYVILSD
     ILGEEDHLGD MDFKVAGTKN GITGFQMDIK ISNVTKQLMR DALEQARIGR MHILSIMDSV
     ISSSRGDISV NAPKIVQLQI DIDKISLVIG STGKTVKAIT DEFEVRVQIE QDGRITLFGT
     DNLKMQKAKA KIESIVREPK VGEIYDGIVK KINSFGAFIE LTPTKEGFLS NRSRSRDDRY
     GSDIRHSRYS NRHSRYGRDN RSSFSMRFPR LEEGQIVKVR ISDIDKFGKI ELELARD
 
 
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