PNP2_ORYSJ
ID PNP2_ORYSJ Reviewed; 982 AA.
AC Q6KAI0; Q0DZI0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase 2, mitochondrial;
DE EC=2.7.7.8;
DE AltName: Full=Polynucleotide phosphorylase 2;
DE Short=PNPase 2;
DE Flags: Precursor;
GN Name=PNP2; OrderedLocusNames=Os02g0617700, LOC_Os02g40460;
GN ORFNames=OJ1014_H03.14;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 661-982.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Involved in the 3'-end maturation of mitochondrial mRNAs,
CC rRNAs and tRNAs. Functions as a poly(A) mRNA 3'-5' degrading
CC phosphorylase (By similarity). {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF09358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003980; BAD21450.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK058997; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q6KAI0; -.
DR SMR; Q6KAI0; -.
DR STRING; 4530.OS02T0617700-01; -.
DR PaxDb; Q6KAI0; -.
DR PRIDE; Q6KAI0; -.
DR eggNOG; KOG1067; Eukaryota.
DR HOGENOM; CLU_044277_0_0_1; -.
DR InParanoid; Q6KAI0; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6KAI0; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 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; 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; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF46915; SSF46915; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50126; S1; 1.
PE 2: Evidence at transcript level;
KW Exonuclease; Hydrolase; Mitochondrion; mRNA processing; Nuclease;
KW Nucleotidyltransferase; Reference proteome; Repeat; RNA-binding;
KW rRNA processing; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..982
FT /note="Polyribonucleotide nucleotidyltransferase 2,
FT mitochondrial"
FT /id="PRO_0000420277"
FT DOMAIN 624..678
FT /note="KH"
FT DOMAIN 689..757
FT /note="S1 motif 1"
FT DOMAIN 920..982
FT /note="S1 motif 2"
FT REGION 792..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 107028 MW; 0B05E5A0E8684351 CRC64;
MSMAVASLRL LARGGRRRAR FPAPLSVPGG RAAFLSGAAE EVAQADAPPP PPPGRKVLES
FREEFEIGGR VISFETGKMA RFANGSVVIS MDDTHVLSTV AAAKSSEPVR DFLPLTVDYQ
EKQYAQGVIP TTYMRREGAP KERELLCGRI IDRPIRPLFP PGFYHEVQVM NATIIMVNVI
SSDGKQDPDV MAANASSAAL MLSDIPWNGP IGVIRVGRID GNFVLNPTVD ELGLSDLNLV
YACSRDKTLM IDVQAREITE RDLQAGMKLA HAEAVKCINP QLRLAKRAGK KKKEYKISLI
SDKSYEKIRT LSEAPIEEVF TDSTYGKFER GEALENITQS VKAKLEEECD EDSLKFLHKA
VDTVRKQVIR KRIIEKGLRV DGRQLDEVRP LYCESSTYPI LHGSALFSRG DTQVLCTVTL
GAPGDAQRLD SIVGPPTKRF MLHYSFPPFS INEVAKRGGL NRREVGHGTL AEKALLAVLP
PEGEFPYTVR VNSEVMASDG STSMASVCGG SMALMDAGIP VREHVAGVSV GLVSEVDQTT
GDISSYRILT DILGLEDHLG DMDFKIAGTR RGITAIQLDI KPAGIPLDII CESLEPARKA
RNQILDRMDQ EISSARAFND GSSPRLATLS FSSDSLRKLL FHRKKIEQET GARVSVSDGT
VTIVAKTQPI MDKAIEKVEF LVGREIEVGR TYKGVVSSIK EYGAFVEFNG GQQGLLHISE
LSHDKVSKVS DVVSVGQVLS LTCIGQDLRG NIKLSLKATL PHAHEKKDLA SNHTDPLPSQ
EVVGWTAVEN MPSKDANAEP SISKDEDNMI EETPGCSTPA VIIRSAAECD AQDVTNDPKK
KRPKVAKSSP KLSKPASERQ EVKRTSAKKT SGASTTAKKN KKEKADSSND VLDAIPEQNK
SNIMNYSSPS NFRSGSMKLG DVVTAKVYQI RAYGLVLELS DGVRGMHKFA ENGHKDFEVG
EELLVKCSSF NAKGIPVFSL LD
