PNP4_ALKMQ
ID PNP4_ALKMQ Reviewed; 704 AA.
AC A6TRK1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase 4 {ECO:0000255|HAMAP-Rule:MF_01595};
DE Short=PNPase 4 {ECO:0000255|HAMAP-Rule:MF_01595};
GN Name=pnp4 {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=Amet_2667;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR48819.1; -; Genomic_DNA.
DR RefSeq; WP_012063792.1; NC_009633.1.
DR AlphaFoldDB; A6TRK1; -.
DR SMR; A6TRK1; -.
DR STRING; 293826.Amet_2667; -.
DR EnsemblBacteria; ABR48819; ABR48819; Amet_2667.
DR KEGG; amt:Amet_2667; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_9; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000001572; 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; 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;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..704
FT /note="Polyribonucleotide nucleotidyltransferase 4"
FT /id="PRO_0000329494"
FT DOMAIN 550..609
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 619..687
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 704 AA; 77579 MW; 8B8AA57435D09D83 CRC64;
MIKQFQTELA GKTLHVEIGK YAEQASGSCM VRYGDTTVLV NATASKSPRE GIDFFPLSVD
YEEKLYAVGK IPGGFIKREA RPSEKAVLTS RLIDRPIRPL FPKGYRNEVQ VIATVMSVDK
DYAPDIVAMI GSSIALSISD IPFGGPTGSV NVGLVNGEFV LNPTSDQRAI SDIDLVVSGT
KDAIMMIESG ANEVTEDQML DALMFAHEEI KTIVAFIEEI VAEVGKPKQE VQLFAIDETL
DMEVRVFAKD KIVTAMKTFD KMERNERLDN VKKEILVHFS KQYENELKSI VEVINSIIKE
QFRYMITHDK VRPDERALDE IRPITSEVGI LPRTHGTGLF TRGQTQVLTV ATLGALGEVQ
ILDGLGEEES KRYMHHYNFP PYSVGEAKFL RGPGRREIGH GALAERALLP MVPSQDDFPY
AIRLVSEVLS SNGSSSQASV CGSTLALLDA GVPIKDMVAG IAMGLVKEND KIAILSDIQG
MEDALGDMDF KVAGTDKGIT AIQMDIKIKG IHKDILKDAL EQARVGRLHI LDKMKKAIDK
PRPELSPFAP RVLKMKIHPD KIRDVIGSGG KTINRIIDET GVKIDIDNDG TIFIAAESQE
AVEKAIIIIE NIIKDPEVGQ NYTGKVIKIM NFGAFLEILP GKEGLLHVSN IAHERVNKVE
DVLEVGQEIE VKVMEIDQQG KINLSRKALL PKESKAENTK EEKA
