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Database: UniProt
Entry: A0A239AJE6_9ACTN
LinkDB: A0A239AJE6_9ACTN
Original site: A0A239AJE6_9ACTN 
ID   A0A239AJE6_9ACTN        Unreviewed;       768 AA.
AC   A0A239AJE6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-JUN-2019, entry version 8.
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=SAMN04488107_0845 {ECO:0000313|EMBL:SNR95650.1};
OS   Geodermatophilus saharensis.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Geodermatophilus.
OX   NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNR95650.1, ECO:0000313|Proteomes:UP000198386};
RN   [1] {ECO:0000313|EMBL:SNR95650.1, ECO:0000313|Proteomes:UP000198386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45423 {ECO:0000313|EMBL:SNR95650.1,
RC   ECO:0000313|Proteomes:UP000198386};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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       ECO:0000256|SAAS:SAAS00360775}.
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, ECO:0000256|SAAS:SAAS01115795};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595, ECO:0000256|SAAS:SAAS00360760};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00360763}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979043}.
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DR   EMBL; FZOH01000001; SNR95650.1; -; Genomic_DNA.
DR   Proteomes; UP000198386; 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; 3.30.230.70; -; 2.
DR   HAMAP; MF_01595; PNPase; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR014069; GPSI/PNP.
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_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; PF00575; S1; 1.
DR   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF46915; SSF46915; 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   TIGRFAMs; TIGR02696; pppGpp_PNP; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000198386};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00274809};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00274808};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00274804};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979037};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979024};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979029, ECO:0000313|EMBL:SNR95650.1}.
FT   DOMAIN      670    739       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION        1     22       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A239AJE6}.
FT   REGION      745    768       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A239AJE6}.
FT   COMPBIAS      1     16       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A239AJE6}.
FT   METAL       533    533       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       539    539       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   768 AA;  81074 MW;  EA2BB7EDDCE2998D CRC64;
     MSAPTTQGSQ TTNGVAAEYD PEDGVTTATA VIDNGSYGSR SVTFETGRLA KQAAGSVVVT
     MGDSMLLSAT TAGRQPKEHF DFFPLTVDVE ERMYAAGRIP GSFFRREGRP SEDAILTCRL
     IDRPLRPTFA KGLRNEVQVV ITVLALDPQH LYDVLAINGA SASTQLSGLP FSGPVGGTRV
     ALVNGQWIGF PTHAELEDAV FDMVVAGRLL PDGDVAIMMV EAEATEKTIQ LVSGGATAPT
     EEVVAQGLEA AKPFIRALCE AQSALAEKAA KPVAEFPRFL DYSDDVYAAV ESAALDRLTQ
     AQSIAGKTER NDATDALKDE VLASLAEQFA GREKEVSAAF RAVTKKVVRQ RILRDKVRID
     GRGVTDIRPL SAEVEVVPRV HGSALFERGE TQILGVTTLN MLRMEQQLDT LSPVTRKRYM
     HNYNFPPYST GETGRVGSPK RREIGHGALA ERALVPVLPD REEFPYAIRQ VSEALGSNGS
     TSMGSVCAST LSLLNAGVPL RAPVAGIAMG LVSDEVDGKT EYVALTDILG AEDAFGDMDF
     KVAGTKDFVT ALQLDTKLDG IPSDVLAQAL TQARAARLHI LDVMNEAIDA PDEMSPYAPR
     VTTVRIPVDK IGAVIGPKGQ MINSIQDETG AEITIEDDGT IYVGASDGPS AQAAVDRINA
     IANPQMPKVG ERFLGTVVKT TPFGAFVSLL PGKDGLVHIS KLGGGKRIGK VEDVVNVGDK
     LQVEITDIDA RGKISLVPVA ADGDGAASGD GAAPSGDQAA PADAPAEA
//
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