(data stored in ACNUC7421 zone)

HOGENOM: VIBSE_1_PE1003

ID   VIBSE_1_PE1003                       STANDARD;      PRT;   711 AA.
AC   VIBSE_1_PE1003; A7K324;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase; EC=2.7.7
DE   8;AltName: Full=Polynucleotide phosphorylase; (VIBSE_1.PE1003).
GN   Name=pnp; OrderedLocusNames=VEA_002613; ORFNames=VEx25_1608;
OS   VIBRIO SP. EX25.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=150340;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS VIBSE_1.PE1003.
CC       Vibrio sp. Ex25 chromosome chromosome 1, complete sequence.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A7K324_VIBSE
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3'- to 5'-direction (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate.
CC   -!- SUBUNIT: Homotrimer. Organized into a structure (processome or RNA
CC       degradosome) containing a number of RNA-processing enzymes (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family.
CC   -!- SIMILARITY: Contains 1 KH domain.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
CC   -!- GENE_FAMILY: HOG000218326 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A7K324; -.
DR   EMBL; CP001805; ACY50775.1; -; Genomic_DNA.
DR   EMBL; DS267823; EDN56960.1; -; Genomic_DNA.
DR   RefSeq; YP_003285240.1; NC_013456.1.
DR   ProteinModelPortal; A7K324; -.
DR   SMR; A7K324; 618-693.
DR   STRING; A7K324; -.
DR   GeneID; 8556341; -.
DR   GenomeReviews; CP001805_GR; VEA_002613.
DR   KEGG; vex:VEA_002613; -.
DR   NMPDR; fig|150340.3.peg.1958; -.
DR   ProtClustDB; PRK11824; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   HAMAP; MF_01595; PNPase; 1; -.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:1.10.10.400; PNPase_PH_RNA-bd_bac/org-type; 1.
DR   PANTHER; PTHR11252; PNPase; 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; 3_ExoRNase; 1.
DR   SUPFAM; SSF55666; 3_ExoRNase; 2.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 2.
DR   TIGRFAMs; TIGR03591; Polynuc_phos; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
DR   HOGENOMDNA; VIBSE_1.PE1003; -.
KW   polyribonucleotide nucleotidyltransferase;
KW   Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
SQ   SEQUENCE   711 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MFEKPVVKTF QYGNHTVTLE TGVIARQATA AVMVTMDDTS VFVSVVGKKE AVAGQDFFPL
     TVNYQERTYA AGKIPGGFFK REGRPSEGET LTARLIDRPI RPLFPDAFKN EVQVIATVMS
     VNPDVQPDIV TMIGTSAALA ISGIPFNGPI GAARVGHIDG QLVLNPSQTE LETSKLDLVV
     AGTESAVLMV ESEADNLTEE EMLAAVVYGH DQQQVAIKAI NEFKAEVATP AWDWVAPEEN
     TALKDKIAEL AEAKLVEAYK ITEKMARYDR INEIAAEVNE VLLAEDPEAD TKEIHTIFHD
     LEKTVVRRSI IAGNPRIDGR EKDMVRALDV RTGVLPRTHG SALFTRGETQ AIVTATLGTQ
     RDAQIIDELT GERKDHFLLH YNFPPYCVGE TGFVGSPKRR EIGHGKLAKR GIAAVMPSVD
     EFPYTVRVVS EITESNGSSS MASVCGTSLA LMDAGVPIKS SVAGIAMGLV KEGDDFVVLS
     DILGDEDHLG DMDFKVAGTN TGITALQMDI KIEGITKEIM QIALNQAQGA RKHILSVMDE
     AISGAREDIS EFAPRIHTMK ISAEKIKDVI GKGGAVIRAL TEETGTTIEI EDDGTIKIAA
     TEGTAAKEAI RRIEEITAEV EVGRIYTGKV ARLADFGAFV TVLPGKDGLV HISQIAEKRV
     EKVSDYLAEG QEVQVKVLEI DRQGRVRLSM KEAVEKPAEE AAAEAPAAKD E
//

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