ID E7A8Q2_HELFC Unreviewed; 679 AA.
AC E7A8Q2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
GN Name=pnp {ECO:0000313|EMBL:CBY82389.1};
GN OrderedLocusNames=Hfelis_03050 {ECO:0000313|EMBL:CBY82389.1};
OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=936155 {ECO:0000313|EMBL:CBY82389.1, ECO:0000313|Proteomes:UP000007934};
RN [1] {ECO:0000313|Proteomes:UP000007934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC {ECO:0000313|Proteomes:UP000007934};
RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA Muller A.;
RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT Helicobacter felis.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBY82389.1, ECO:0000313|Proteomes:UP000007934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC {ECO:0000313|Proteomes:UP000007934};
RX PubMed=21402865;
RA Arnold I.C., Zigova Z., Holden M., Lawley T.D., Rad R., Dougan G.,
RA Falkow S., Bentley S.D., Muller A.;
RT "Comparative whole genome sequence analysis of the carcinogenic bacterial
RT model pathogen Helicobacter felis.";
RL Genome Biol. Evol. 3:302-308(2011).
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; FQ670179; CBY82389.1; -; Genomic_DNA.
DR RefSeq; WP_013468761.1; NC_014810.2.
DR AlphaFoldDB; E7A8Q2; -.
DR STRING; 936155.HFELIS_03050; -.
DR GeneID; 36134252; -.
DR KEGG; hfe:HFELIS_03050; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_7; -.
DR Proteomes; UP000007934; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
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 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_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; 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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CBY82389.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007934};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBY82389.1}.
FT DOMAIN 612..679
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 679 AA; 74872 MW; 44A55BC200565AD6 CRC64;
MTIRIHHEEY RLNDIAKQAT SALLYRHKGC VILATIMVDK ACVEENFLPL SVHFSQRAYA
IGRIPGGFNK REGKLSEFET LTSRAIDRSL RPLFAKDYAH PTQITLLVLS HDQQSDLQVC
ALHAAANALY LANLGIENVA AVRVGRIGGK IVYNPNATEL QKSDLNLYVS GTSEALLMVE
MHSQESLPEA TLLDLLEKAQ KHIRENCLQF QKSFAPHRKA PLAINTPTPP NPTLELLLKQ
HFHQQILEIK TQMAKSEREV DFAHLTTAIA HTLQEKGHSY TFEQIQRSLE RYTHQCIREE
ILHTKTRPDG RGFETIRPIS IETNLLPHCH GSALFTRGHT QALVVCTVGG PNDAKLQENL
DGLHKERFMF HYNFPPFSVG EATPLSAPGR REIGHGNLAK CALQGSILES DQTIRLVSEI
LESNGSSSMA SVCGGSLALY ASGIKLKSLI AGVAMGLIIQ GEETAILSDI SALEDMQGDM
DFKIAGNLEG VVALQMDTKI AGLSLALLSQ ILQQAKEARG AILECMEQAI EGIMPNTDAL
PTQESFSVPP KKIATIIGPS GKSIKEIIER FEVQIELDKT SGAVCISGGA QNVLDAKEYI
LEMTGFQPYH VEEVLEVEIK KVVDFGIFVR LPRGGDALLH KSHLEKRDLD KDSFMENNTL
ECRIIAIHDD SGKIDVDLA
//
