PNP_MYCS2
ID PNP_MYCS2 Reviewed; 763 AA.
AC A0QVQ5; I7G725;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; Synonyms=gpsI;
GN OrderedLocusNames=MSMEG_2656, MSMEI_2593;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK73464.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39061.1; -; Genomic_DNA.
DR RefSeq; WP_011728507.1; NZ_SIJM01000064.1.
DR RefSeq; YP_886993.1; NC_008596.1.
DR PDB; 7LD5; EM; 3.07 A; A/B/C=1-763.
DR PDBsum; 7LD5; -.
DR AlphaFoldDB; A0QVQ5; -.
DR SMR; A0QVQ5; -.
DR STRING; 246196.MSMEI_2593; -.
DR PRIDE; A0QVQ5; -.
DR EnsemblBacteria; ABK73464; ABK73464; MSMEG_2656.
DR EnsemblBacteria; AFP39061; AFP39061; MSMEI_2593.
DR GeneID; 66734065; -.
DR KEGG; msg:MSMEI_2593; -.
DR KEGG; msm:MSMEG_2656; -.
DR PATRIC; fig|246196.19.peg.2622; -.
DR eggNOG; COG1185; Bacteria.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR BRENDA; 2.7.7.8; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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; 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; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18955433"
FT CHAIN 2..763
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329720"
FT DOMAIN 592..651
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 663..732
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 739..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 24..34
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:7LD5"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7LD5"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 184..195
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 241..257
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 273..291
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 296..313
FT /evidence="ECO:0007829|PDB:7LD5"
FT TURN 314..320
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 322..344
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 405..413
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:7LD5"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:7LD5"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 471..484
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 494..507
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 510..520
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:7LD5"
FT STRAND 539..549
FT /evidence="ECO:0007829|PDB:7LD5"
FT HELIX 556..580
FT /evidence="ECO:0007829|PDB:7LD5"
SQ SEQUENCE 763 AA; 81027 MW; 0F11A001A82BAC12 CRC64;
MSVVELEDGV YESTAVIDNG SFGTRTIRFE TGRLAQQAAG SAVAYLDDET MLLSATTASK
NPKDHFDFFP LTVDVEERMY AAGRIPGSFF RREGRPSTDA ILTCRLIDRP LRPSFVDGLR
NEIQVVVTVM SLDPKDLYDV LAINAASMST QLAGLPFSGP VGGARIALID GTWVAFPTVE
QLERAVFDMV VAGRIVGDGD SADVAIMMVE AEATENVVEL VAGGAQAPTE AVVAEGLEAA
KPFIKALCAA QQELADRAAK PAGEYPVFPD YEADVYDAVA SVATEALAEA LTIAGKTERN
DRTDEIKVEV LERLAEPYAG REKEIGAAFR SLTKKLVRQR ILTDHFRIDG RGITDIRALS
AEVAVIPRAH GSALFERGET QILGVTTLDM IKMAQQIDSL GPENTKRYMH HYNFPPYSTG
ETGRVGSPKR REIGHGALAE RALVPVLPSI EEFPYAIRQV SEALGSNGST SMGSVCASTL
ALLNAGVPLK APVAGIAMGL VSDDVDVDGK VEKRYVALTD ILGAEDAFGD MDFKVAGTKD
FVTALQLDTK LDGIPSQVLA GALSQAKDAR LTILDVMAEA IDRPDEMSPY APRITTIKVP
VDKIGEVIGP KGKMINSITE ETGAQISIED DGTVFVGAAD GLSAQAAIDK INAIANPQLP
KVGERFLGTV VKTTDFGAFV SLLPGRDGLV HISKLGKGKR IAKVEDVVKV GDKLRVEIAD
IDNRGKISLV LVAEESAESA ESAGDKGAEK AEGAAADVTP AEA
