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Database: UniProt
Entry: R7JZE7_9CLOT
LinkDB: R7JZE7_9CLOT
Original site: R7JZE7_9CLOT 
ID   R7JZE7_9CLOT            Unreviewed;       695 AA.
AC   R7JZE7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   16-JAN-2019, entry version 28.
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=BN584_00463 {ECO:0000313|EMBL:CDE69036.1};
OS   Clostridium sp. CAG:277.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium; environmental samples.
OX   NCBI_TaxID=1262790 {ECO:0000313|EMBL:CDE69036.1, ECO:0000313|Proteomes:UP000018281};
RN   [1] {ECO:0000313|EMBL:CDE69036.1, ECO:0000313|Proteomes:UP000018281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:277 {ECO:0000313|Proteomes:UP000018281};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01595}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDE69036.1}.
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DR   EMBL; CBJK010000070; CDE69036.1; -; Genomic_DNA.
DR   Proteomes; UP000018281; 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   Gene3D; 3.30.1370.10; -; 1.
DR   Gene3D; 3.30.230.70; -; 2.
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_S5_D2-typ_fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR11252; PTHR11252; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF03726; PNPase; 1.
DR   Pfam; PF01138; RNase_PH; 2.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   Pfam; PF00575; S1; 1.
DR   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   SUPFAM; SSF55666; SSF55666; 2.
DR   TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018281};
KW   Cytoplasm {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|HAMAP-Rule:MF_01595};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018281};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01595};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000313|EMBL:CDE69036.1}.
FT   DOMAIN      624    692       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   METAL       487    487       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       493    493       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   695 AA;  77003 MW;  A38756A96F78D395 CRC64;
     MAYKTYSMEL AGRTLSIDIG RVAKQANGAA LMHYGDTTVL CTATASEKPR EGIDFFPLSV
     EFEEKMYSVG KIPGGFNKRE GKASENAVLT ARVIDRPMRP LFPKDYRNDC SLNNLVLSVD
     PECRPELVAM IGSAVATSIS DIPFYGPCAT TQMGMVDGEF IVNPSQEVWD NGDLRLTVAS
     TAEKVIMIEA GANEIPEDKM IEAIYKCHDV NQTIIALINQ MVEEIGKPKH EYTSCAIPEE
     MFEEIKKIVP PAEMEEAVFS DDKQTREENV RQVTEKLAEA FAEKEDWLEI LDEAVYQYQK
     KTVRKMILKD HKRPDGREIT QIRPLAAEVD LIPRVHGSAM FTRGQTQICN ITTLAPLSEK
     QRIDGLDANK TEKRYMHHYN FPSYSVGETK PSRGPGRREI GHGALAEKAL LPVLPSEEEF
     PYAIRSVSET FESNGSTSMA STCASCMSLM AAGVPIKKMV AGISCGLVTG ETDDDFVLLT
     DIQGLEDFFG DMDFKVTGTE DGITAIQMDI KIHGLTRPIV EGAIARCREA RMFIMDTCMK
     PAISEPREKV GQYAPKIIQI MIDPQKIGDV VGQRGKTINA LIERTGVKID INDEGQVSIC
     GEDEAMMNEA KRLIEIITTD FHQGQILEGD VVSIKEFGAF VEFAPGKEGM VHISKIAKER
     INHVEDVLTL GDHVKVVCLG KDKMGRMSFS IKDVK
//
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