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Database: UniProt
Entry: A0A1H6M8H8_9FLAO
LinkDB: A0A1H6M8H8_9FLAO
Original site: A0A1H6M8H8_9FLAO 
ID   A0A1H6M8H8_9FLAO        Unreviewed;       755 AA.
AC   A0A1H6M8H8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05421793_1624 {ECO:0000313|EMBL:SEH95215.1};
OS   Epilithonimonas hominis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Epilithonimonas.
OX   NCBI_TaxID=420404 {ECO:0000313|EMBL:SEH95215.1, ECO:0000313|Proteomes:UP000198555};
RN   [1] {ECO:0000313|Proteomes:UP000198555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19326 {ECO:0000313|Proteomes:UP000198555};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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: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:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC         EC=2.7.7.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC       Rule:MF_01595}.
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DR   EMBL; FNWX01000062; SEH95215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6M8H8; -.
DR   STRING; 420404.SAMN05421793_1624; -.
DR   Proteomes; UP000198555; 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   CDD; cd02393; KH-I_PNPase; 1.
DR   CDD; cd11363; RNase_PH_PNPase_1; 1.
DR   CDD; cd11364; RNase_PH_PNPase_2; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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; IPR036456; PNPase_PH_RNA-bd_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR03591; polynuc_phos; 1.
DR   PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01595};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01595}.
FT   DOMAIN          633..699
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          696..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         494
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         500
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   755 AA;  83830 MW;  E4FD8CCFAF669ADB CRC64;
     MSAPQAITEL ITLADGREIT IETGKLAKQA DGSVVVKMGG TMLLATVVAN KEANPGVDFL
     PLTVDYREKF YAGGKIPGNF FRREARPSDQ EILTMRLVDR VLRPLFPEDF HAEVQVMISL
     ISYDGQSIPD DLAGLAASSA IAITDIPFNG PMSEVRVVRI DGQLSINPKF EDLAKSDLDI
     MVGATKDSIV MVEGEMKEIT EAEMLEAITF AHEEIKKQVE AQERLAQKVG KSFPKREYNH
     ENHDEAIREK VWKETYDKVY EVAKTPSSKE ERGEKFKAVR DEFLAQYVED AEELERVTPF
     VKVYYHDVEK EAMRQMILND KIRLDGRDPE TIRPIWSEID YLPGAHGSAI FTRGETQSLT
     AVTLGSVKDG NMVDSVMANY DERFFLHYNF PPFSTGEARP LRGTSRREVG HGNLAQRALA
     NMIPEENPYT IRIVSDILES NGSSSMATVC AGTLALMDAG VQIKKPVSGI AMGLVTDVKT
     GKFTVLSDIL GDEDHLGDMD FKVTGTADGI TACQMDIKIQ GLSMDIMEKA LLQAREGRLH
     ILDKITETIA QPREDVKPHA PKMVMMEIPK DFIGAVIGPG GKIIQQMQKD TDTVIAIEEV
     GEIGRIEISG VSREKINEAV AKINEITFVP VVGEVYQGKV VKVMDFGAFV AIAKGTEGLL
     HISEIEWARL DKVPYKEGDE VEVKFMGYDD RKKMKLSRKV LLPRPPRPEK KEGEQRGPRP
     EGQNRSDRSA RPEGNRRPEG EGEKPAGEHN PSNEA
//
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