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Database: UniProt
Entry: A0A0M4LXW0_9ACTN
LinkDB: A0A0M4LXW0_9ACTN
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ID   A0A0M4LXW0_9ACTN        Unreviewed;       747 AA.
AC   A0A0M4LXW0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
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=AL705_00975 {ECO:0000313|EMBL:ALE18527.1};
OS   Lawsonella clevelandensis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Lawsonella.
OX   NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE18527.1, ECO:0000313|Proteomes:UP000068137};
RN   [1] {ECO:0000313|EMBL:ALE18527.1, ECO:0000313|Proteomes:UP000068137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1698 {ECO:0000313|EMBL:ALE18527.1,
RC   ECO:0000313|Proteomes:UP000068137};
RX   PubMed=26659691;
RA   Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT   "Complete Genome Sequences for Two Strains of a Novel Fastidious,
RT   Partially Acid-Fast, Gram-Positive Corynebacterineae Bacterium,
RT   Derived from Human Clinical Samples.";
RL   Genome Announc. 3:e01462-15(2015).
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; CP012390; ALE18527.1; -; Genomic_DNA.
DR   RefSeq; WP_053961422.1; NZ_CP012390.1.
DR   EnsemblBacteria; ALE18527; ALE18527; AL705_00975.
DR   KEGG; cbq:AL705_00975; -.
DR   PATRIC; fig|1528099.3.peg.200; -.
DR   KO; K00962; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000068137; Chromosome.
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:UP000068137};
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   Reference proteome {ECO:0000313|Proteomes:UP000068137};
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}.
FT   DOMAIN      671    740       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   METAL       534    534       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       540    540       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   747 AA;  80471 MW;  1D51AD17F510ADA3 CRC64;
     MTELREFEVE EGVFETETTI DNGAFGTRNV RFETGRLAKQ AAGSAVVYLD DETMMLSCTT
     ASKQPREGFD FFPLTVDVEE RMYAAGRIPG NFFRREGRPT TDAILTCRLI DRPLRPSFVS
     GLRNEVQVVV TMLSLRPGDI YDCVAINAAS CSTQLAGLPF SGPVGGVRIA LIPTESNPEG
     QWVCFPTVEQ LKMAVFNMAV AGRIVSEDDG TGSPEIAIMM VEAGATEEVV ELVGGGAQAP
     TEEVVAGGLE AAKPFIAQLC QAQQQLAGVA AKETAEFPLY PAYQDDSFEA VEKAATAELE
     KIYTIADKQE REAADTELKE KVFEELAEQF EGRESEIGGA YKAITKKIIR QRILKDHFRI
     DGRDVTDIRA LSAEVEVIPR AHGSSLFERG ETQIMGVTTL DMLKMEQQID SLGPEESKRY
     IHHYNFPPYS TGDTGRVGSP KRREIGHGAL AERALLPMIP SREDFPYAIR QVSEALGSNG
     STSMGSVCAS TMSLLNAGVP LKAPVAGIAM GLVSDEVDGE MQYQALTDIL GAEDAFGDMD
     FKVAGTKDFI TALQLDTKLD GIPSHVLAAA LTQARDARLT ILDVMNEAID APDELSPYAP
     RITSIQIPVD KIGEVIGPKG KQINAITEET GANISIEDDG TVYVSATNGD AAQAAIDLIN
     AIANPQLPKV GERFLGTVVK TTAFGAFVSL LPGRDGLVHI SKLGKGKRIA KVEDVVNVGD
     KLQVEIADID KRGKISLVPV DDSDDNE
//
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