ID A0AA38M7I4_9CUCU Unreviewed; 746 AA.
AC A0AA38M7I4;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE AltName: Full=Polynucleotide phosphorylase 1 {ECO:0000256|ARBA:ARBA00031451};
GN ORFNames=Zmor_023625 {ECO:0000313|EMBL:KAJ3646013.1};
OS Zophobas morio.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Zophobas.
OX NCBI_TaxID=2755281 {ECO:0000313|EMBL:KAJ3646013.1, ECO:0000313|Proteomes:UP001168821};
RN [1] {ECO:0000313|EMBL:KAJ3646013.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=QUZm001 {ECO:0000313|EMBL:KAJ3646013.1};
RX PubMed=37002914; DOI=10.1093/g3journal/jkad079;
RA Kaur S., Stinson S.A., diCenzo G.C.;
RT "Whole genome assemblies of Zophobas morio and Tenebrio molitor.";
RL G3 (Bethesda) 13:jkad079-jkad079(2023).
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ3646013.1}.
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DR EMBL; JALNTZ010000007; KAJ3646013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA38M7I4; -.
DR Proteomes; UP001168821; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:TreeGrafter.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IEA:TreeGrafter.
DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IEA:TreeGrafter.
DR CDD; cd09033; KH-I_PNPT1; 1.
DR CDD; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR FunFam; 3.30.1370.10:FF:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000032; Polyribonucleotide nucleotidyltransferase 1; 1.
DR FunFam; 2.40.50.140:FF:000113; polyribonucleotide nucleotidyltransferase 1, mitochondrial; 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 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 NCBIfam; NF008805; PRK11824.1; 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; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP001168821};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 668..739
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 746 AA; 83032 MW; FD3E178402724E31 CRC64;
MFLITRKNPL KRTAKLKHNL NTVRCFSERL TSPEVDINFN NGRSLKISTG QYARLADGCA
VATLGDTSVM VTAVSKTKAS PSNFLPLVVD YRQKSAAAGR IPTNFFRREL GPSEREILTS
RLIDRSLRPL FPEHFNYDTQ VVCNMLAVDS VNNPDVISIN AASAALALSD IPWNGPVGAV
RLGFIDNEVI INPTRKELQS SSLNLVLSAT KRNLVVMLEG NANSIFQQDL QKAIKLGTKE
TQHVISGIEA LQKAFGKQKR ELVPVTEASE EVNEAVRSLC EMRVRKIFTD YTHDKLSRDN
ALSDVRTDVV EKMKANFPDL DPNLLNETYN KIVKQIFRDL IFEEEKRCDG RLYDELRNIE
CKVNLYKPLH GSAMFQRGQT QVFCTVTLDS HESAMRMDPM AMLISGVKEK NFFLHYEFPP
FATKETGRIG PIGRREIGHG ALAEKGLTPS IPDDFPFTIR LTSEVLESNG SSSMASVCGG
TLALMDAGVP ITAPAAGVAI GLVTRYDQER KNIEDYRLLT DLLGIEDYMG DMDFKIAGTK
KGITALQADI KIPGLPLKIV MEAIQKATDA KHKIFQIMHE CIDKPRTIKK DNWPVSEKLE
VEPHKRSKLI GMGGMNLKKL FAETGVQVSP LDDNTFEIFA PNQSAMDEAQ EFINKLLTAE
RVPELEFGGI YSANIVEIRD IGVMVTLYPG MPPALLHNSQ LDQRKVAHPS ALDLQVGQEI
QVKYFGRDPV SGLMRLSRKV LQAPPK
//
