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PNP_THETH
ID   PNP_THETH               Reviewed;         713 AA.
AC   Q9ZAE1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE   AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN   Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RA   Serganov A.A., Garber M.B., Portier C.;
RT   "Polynucleotide phosphorylase from Thermus thermophilus: cloning,
RT   sequencing and expression of the gene and biochemical properties of the
RT   enzyme.";
RL   Submitted (JAN-1997) 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:0000255|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:0000255|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR   EMBL; Z84207; CAB06341.1; -; Genomic_DNA.
DR   RefSeq; WP_011173207.1; NZ_CP053287.1.
DR   AlphaFoldDB; Q9ZAE1; -.
DR   SMR; Q9ZAE1; -.
DR   BRENDA; 2.7.7.8; 2305.
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; 2.40.50.140; -; 1.
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; 2.
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; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
FT   CHAIN           1..713
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000329915"
FT   DOMAIN          565..631
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          633..701
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         498
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         504
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   713 AA;  78193 MW;  2979859D9AC5EA82 CRC64;
     MEGTPNVPQA HRYELTLAGR PLVLETGKYA KQASGSVLVR YADTVVLATA QASETPVEAD
     FLPLTVEFEE RHYAVGKIPG SFMRREGRPG EKAILSARMT DRPIRPLFPK GFRHEVQIIV
     TVLSADQKNP PDILGPIAAS AALMLSDIPW EGPIAAVRVG LIGGSFVLNP TLQELEESQL
     DLVVAGSKEA ILMVEAEAGE VDEETLVQAL EFAHKEMQPI LELQEAMARE LAKPKMAWTP
     PESLPEEEKE ALYRLALERG LSQVLQTASK GERSRALAEF AERLIAEALP KGEDGTPDEG
     KKPLYESAFD EVVRRELRRL VLEEGKRADG RGPKDLRPIW IEVDVLPRAH GSAVFTRGET
     QVLGTVTLGT GRDEQILDDL GIDETEKFLV HYNFPPFSTG EVRRLRGVSR REVGHGNLAK
     RALKAVMPKE EDFPYTIRVV GDVLESNGSS SMATVCAGCL ALMDAGVPIR APVAGVAMGL
     VWEENRAVIL TDILGLEDAL GDMDFKVAGT RKGVTALQMD NKVGGLPREV LKEALLQARE
     ARLKILDLME TVLPAPRPEL KPFAPRILSL KVPVEKIGLV IGPGGKNVRA LEELGVEVDI
     EEDGTVRIYS SDLNAALEAK KRIEDLTREA KVGEIYEGTV TRITPFGAFI SLFPGTEGLL
     HISQIAPGRV ERVEDHLKVG DVIKVKVHRI DERGKIDLIR PELEGKIPPR RRK
 
 
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