ID A0A7D5NGL2_9DELT Unreviewed; 724 AA. AC A0A7D5NGL2; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 02-JUN-2021, entry version 4. 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}; OS Cystobacter sp. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Cystobacter; unclassified Cystobacter. OX NCBI_TaxID=1965334 {ECO:0000313|EMBL:QLH55451.1}; RN [1] {ECO:0000313|EMBL:QLH55451.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cbvi35 {ECO:0000313|EMBL:QLH55451.1}; RX PubMed=32639716; RA Hug J.J., Dastbaz J., Adam S., Revermann O., Koehnke J., Krug D., RA Muller R.; RT "Biosynthesis of cittilins, unusual ribosomally synthesized and post- RT translationally modified peptides from Myxococcus xanthus."; RL ACS Chem. Biol. 0:0-0(2020). 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:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:83400; CC EC=2.7.7.8; Evidence={ECO:0000256|ARBA:ARBA00001732, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN731363; QLH55451.1; -; Genomic_DNA. 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; 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; 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; 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 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|ARBA:ARBA00022842, 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 623..691 FT /note="S1 motif" FT /evidence="ECO:0000259|PROSITE:PS50126" FT REGION 692..724 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 487 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595" FT METAL 493 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595" SQ SEQUENCE 724 AA; 78275 MW; C33493821887787E CRC64; MHLKKSVKIG DTELSIETGH MAKQADGAVV VRYGDTVLLV TAVSAREKKD VDFLPLTVEY QEKLYSAGRI PGSYFKREGR LTEKETLASR IVDRSCRPLF PEGYAYETQI ITSVISADPE HEGDIHGITG ASAALWVSDI PFNGPIAGIR VGRVDGKLIA NPTSKQREQS DIDLVMAVSR EAIVMVEGGA EEVSEADMVA ALEFGKQAVQ PALDLQDEMR RTLNKTVRNY DRIPAVAEDL KAKVRALAWD GIVQGYTIKE KAARYDALSK AKKEALSKLK EQLGEAFTSQ VEKHAKSVVE DLKYEHMRTL TVNGGRIGGR GHDKVRDITN EVSVLPRTHG SALFTRGETQ ALVVATLGTS EDEQRLELLG GMSFKRFMLH YNFPPFSVNE TKPLRGPGRR EVGHGALAER ALRNMLPPSD KFPYTVRLVS DILESNGSSS MASVCGGTLA LMDAGVPIKA PVAGIAMGLV KEGDQVAILS DILGDEDHLG DMDFKVCGTS KGITSIQMDI KITGLTTEIM SRALEQARQG RLHILGEMLK TMAEPRKEIS AYAPRITTIQ IRPEFIKNVI GPGGKVIKDI IARTGAVINI DDSGRVDIAS SNVDSVKAAI AMIQALTREA EIGKIYTGTV RKIAEFGAFV ELFPGTDGLI HISELSDKRV KSVSDVLNEG DEVLVKVISI DKTGKIRLSR KEAMAERAAT QQGAAAPAPT ETAPAGATQP GAKA //