ID A0A0U3HG14_9MICC Unreviewed; 754 AA.
AC A0A0U3HG14;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000256|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000256|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000256|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000256|HAMAP-Rule:MF_01595,
GN ECO:0000313|EMBL:GEO93530.1};
GN ORFNames=AS188_08410 {ECO:0000313|EMBL:ALU39768.1}, KFL01_28360
GN {ECO:0000313|EMBL:GEO93530.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU39768.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU39768.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU39768.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO93530.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO93530.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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:0000256|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:0000256|HAMAP-Rule:MF_01595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC Rule:MF_01595}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013254; ALU39768.1; -; Genomic_DNA.
DR EMBL; BJZR01000128; GEO93530.1; -; Genomic_DNA.
DR RefSeq; WP_058858477.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U3HG14; -.
DR STRING; 446860.AS188_08410; -.
DR KEGG; kfv:AS188_08410; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; Unassembled WGS sequence.
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 CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR CDD; cd04472; S1_PNPase; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR NCBIfam; TIGR02696; pppGpp_PNP; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01595};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01595};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000057181};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01595}.
FT DOMAIN 665..737
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 754 AA; 80335 MW; A8DDC6A2CFEAB13C CRC64;
MEGPEIQYAE AVIDNGSYGK RTVRFETGRL AKQAAGAALV TIDEDTTLLS ATTVGKSPRE
GFDFFPLTVD VEERMYAAGR IPGSFFRREG RPSTDAILTC RLIDRPLRPA FGKGIRNEVQ
VVVTVLSINP DEIYNTVAIN AASMSTSLSG MPFQGPIGGV RMALMAGPGG THQWVAFPKH
SQLENAVFDM AVAGRVVTGA DGTEDVAIMM VEAEATDNSW ELIKADGAVA PTEELVAEGL
EAAKPFIKAL CDAQADLKAR AARPALELPR FGGFGDDVRD AVAQAAGTRL AEVYSIAGKQ
EREAATDELH HAVLAELTGE GRPFADRKDE VNGAYQALTK HTVRQRILTE QVRIDGRGLT
DIRQLTAEVE VLPRVHGSAI FERGETQIMG VTTLNMLKME QQIDSLSPVK TKRYVHHYNF
PPYSTGETGR VGSPKRREIG HGALAERAIT PVLPSREEFP YAIRQVSEAL GSNGSTSMGS
VCASTLSLLN AGVPLRAPVA GIAMGLVSDE VDGETRYAAL TDILGAEDAL GDMDFKVAGT
AEFVTAIQLD TKLDGIPSSV LDAALTQARE ARLHILEVMT GAISEPDEMS EFAPRVISVT
VPVSKIGEVI GPKGKMINQI QEDTGTDISI EDDGTVYIGA TDGPSAEAAR AAINAIANPQ
VPEVGERYLG TVVKTTAFGA FVSLTPGKDG LLHISELRKL NEGKRVTDVE DVLGVGQKVQ
VEITKVDDRG KLSLAPVVAE EPGEAAEAEP ADQD
//
