ID T1CZ58_9HELI Unreviewed; 684 AA.
AC T1CZ58;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=HFN_1839 {ECO:0000313|EMBL:GAD18241.1};
OS Helicobacter fennelliae MRY12-0050.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1325130 {ECO:0000313|EMBL:GAD18241.1, ECO:0000313|Proteomes:UP000018143};
RN [1] {ECO:0000313|EMBL:GAD18241.1, ECO:0000313|Proteomes:UP000018143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRY12-0050 {ECO:0000313|EMBL:GAD18241.1,
RC ECO:0000313|Proteomes:UP000018143};
RA Rimbara E., Matsui M., Mori S., Suzuki S., Suzuki M., Kim H., Sekizuka T.,
RA Kuroda M., Shibayama K.;
RT "Draft Genome Sequence of Helicobacter fennelliae Strain MRY12-0050,
RT Isolated from a Bacteremia Patient.";
RL Genome Announc. 1:e00512-13(2013).
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:GAD18241.1}.
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DR EMBL; BASD01000004; GAD18241.1; -; Genomic_DNA.
DR RefSeq; WP_023946687.1; NZ_BASD01000004.1.
DR AlphaFoldDB; T1CZ58; -.
DR STRING; 1325130.HFN_1839; -.
DR eggNOG; COG1185; Bacteria.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000018143; 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; cd00164; S1_like; 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; 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_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 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; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|HAMAP-Rule:MF_01595};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000018143};
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 617..684
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 684 AA; 75834 MW; 024DDB16E3D6247D CRC64;
MHSIDITLEN LNENYKLNYV AKQACGSVLY QNGGTIILAS VAIEKQRVQE DFLPLTVQYI
QKAYANRKIP GGFIKREGKP SEFEILTSRI IDRTLRPIFP KGYYYPTQIT ILVLSYDGIC
DLQVCALHAA ANALLISGLE FVPPISSVRI GKIGDEFVIN PTKNDLKQST LDLYVSGSYS
DVLMIEMKGS DENLDEEDLL KAIKIAQKTI ALDSQKFSDY LLPLKNPILT LPLLDIQTYP
EIYALIQKQY DEQVQQALLA MSKSERSDGL NLIALQIATQ NPQYDIANIT DMLNLYKKHK
VRSLILKLHK RADGRGLEDV RPITIETNIL PCAHSSALFT RGQTQALVVC TLGSDNDAQI
QEDLSGSTKE KFMFHYNFPG FSVGEASPIG SVGRRELGHG NLAKRALESS IIDSPYTIRL
VSEILESNGS SSMASVCGGS LALRACGFYN ELVAGVAMGL VIENDEYAIL TDIMGLEDHD
GDMDFKVAGT RHNITAMQMD IKLGGLDFDI LKEALYQAKR ARIKILDKME EASLEIVINE
NVLPKTETFS VPNGKIVDII GQGGKTIKEI IEKFGVSIDL NREKSEVQIN ADSKESLLEA
KQYILKIVGT QPQYKIGEVF EGVIKKVADF GVFVELPCGN ADGLLHISRI PKTNESIYTR
FHEGQRLKCQ IYGTFKGKIE LSLA
//
