ID F9EFW6_9ACTO Unreviewed; 788 AA.
AC F9EFW6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:EGQ73960.1};
GN ORFNames=HMPREF9062_1338 {ECO:0000313|EMBL:EGQ73960.1};
OS Actinomyces sp. oral taxon 448 str. F0400.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=888056 {ECO:0000313|EMBL:EGQ73960.1, ECO:0000313|Proteomes:UP000005351};
RN [1] {ECO:0000313|EMBL:EGQ73960.1, ECO:0000313|Proteomes:UP000005351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0400 {ECO:0000313|EMBL:EGQ73960.1,
RC ECO:0000313|Proteomes:UP000005351};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAY-2011) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGQ73960.1}.
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DR EMBL; AFQC01000047; EGQ73960.1; -; Genomic_DNA.
DR RefSeq; WP_009749237.1; NZ_GL985606.1.
DR AlphaFoldDB; F9EFW6; -.
DR STRING; 888056.HMPREF9062_1338; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_11; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000005351; 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; SSF50249; Nucleic acid-binding proteins; 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:UP000005351};
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 657..729
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 739..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 788 AA; 84896 MW; DE0597FE01CF5DFB CRC64;
MFIDDPEVTA AEAVIDNGPF GKRVVRFETG RLAKQAAGSA MAYLDGETAV LSATTVGKHP
KEQFDFFPLT VDVEERQYAA GRIPGSFFRR EGRAGTSAIL ACRLIDRPLR PSFVKGLRNE
VQVVETVLAI DPDDAYDVLA INAASMSTQI AGLPFSGPIA GTRLALIDGR WVAFPRYSEI
ERATFNMVVA GRLLDGGDVA IMMVEAGATE NAWSLIAAGA TAPTEAVVAE ALEAAKPHIR
VLCEAQMEVA AHASKPTAEF PLYLDYTDEQ YAAVEEAARA HDLAGAIAAE GKQARDAATD
AVREKVLVDL AERFTSEEDV KALKAAFRAV TKKLVRHRTL TEGVRIDGRG LKDIRTLGAE
VEVLPRVHGS AVFERGETQI LGVTTLNMLR MEQQIDDLSP VTHKRYMHQY IFPPFSTGET
GRVGAPKRRE IGHGALAERA LVPVLPGRDE FPYAIRQVSE ALGSNGSTSM GSVCASTLSL
LQAGVPLRAP VAGIAMGLMH EEIDGETAWA TLTDILGSED AFGDMDFKVA GTRDVITALQ
LDTKLDGLPS DILAGALGQA RDARLFILDV LARAIDGPDE MAPTAPRVLT VRIPVDKIGE
VIGPKGKMIN QIQEDTGADL TVEDDGTVYI GAADGPSAEA AREAVNAIAN PQMPEIGERF
VGTVVKTTTF GAFVSLTPGK DGLLHISQIR RLVGGKRVEN VEDVLNVGDK VQVELAEIDQ
RGKLSLHAVL SDEQLAAEAE NTAGKAVRDG ERRERRPRRE RSGADGERRE RRPRRRRMRT
ADSPSEEE
//
