ID E0VCX0_PEDHC Unreviewed; 708 AA.
AC E0VCX0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 Name=8238083 {ECO:0000313|EnsemblMetazoa:PHUM098920-PA};
GN ORFNames=Phum_PHUM098920 {ECO:0000313|EMBL:EEB11226.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB11226.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB11226.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB11226.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB11226.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM098920-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM098920-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; AAZO01001184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235066; EEB11226.1; -; Genomic_DNA.
DR RefSeq; XP_002423964.1; XM_002423919.1.
DR AlphaFoldDB; E0VCX0; -.
DR STRING; 121224.E0VCX0; -.
DR EnsemblMetazoa; PHUM098920-RA; PHUM098920-PA; PHUM098920.
DR GeneID; 8238083; -.
DR KEGG; phu:Phum_PHUM098920; -.
DR CTD; 8238083; -.
DR VEuPathDB; VectorBase:PHUM098920; -.
DR eggNOG; KOG1067; Eukaryota.
DR HOGENOM; CLU_004217_2_2_1; -.
DR InParanoid; E0VCX0; -.
DR OMA; RFMFHYN; -.
DR OrthoDB; 937144at2759; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd09033; KH-I_PNPT1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 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 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 ECO:0000313|EMBL:EEB11226.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEB11226.1}.
FT DOMAIN 619..690
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 708 AA; 78163 MW; C7FA77FA9D8D8249 CRC64;
MIIGAGKLAK FTDGCATVTF KDTTVMATAV SSDKGGMYSG FVPLTVSFQQ KAAALGRIPL
NFLRRELGQN ENEILISRMI DRSLRPLFPA NFNNETQIVC NPLAMDGENF PDVLSINAAS
AALAVSNIPW NGPVGAVRVG LVDDNIIINP DKNLLSKSSL NLVVVSKAKH YVVMLEGSCS
NILLNDLLRA IKKGVSECQK IIISIEHLAS LCGKPKKEVN ISEINEELYQ SIQMLASEPL
NKIFQNSIHD KLSRDTAISE VRTLIEKKFS DKCENFNQIF SLVCKEVFRN YILINNIRCD
GRLPVELRNI ECESNLFKPL HGSALFQRGQ TQVFCTVALD SPSSALKMDR ISMLTSGLKE
KNFFVHYEFP PFATKEIGKL GPIGRREIGH GSLAEKALKA NIPENFPFTI RLTSEVLESN
GSSSMATVCG GTLALLDAGV PLIKECAGVA MGVVTKWDDD KSGIIDYVIL TDILGIEDYF
GDMDMKVAGT KNHITAIQMD VKTPGLPIKI VMESITQAKQ AISTTLTRMF KDVDLQKKVK
KDNWPVIEKL NVPVNQRAKF IGPGGINIKN FEMKTGVEIT EENLGEFQIF AANKEALNEA
MKIINEKINS QKEPVLEFGA IYTATITEIR EHGCMVILYP AMQPVLIPVT QLDHKKVSHP
SALNLKVGDQ FKVKYFGRDP ISGYMRLSRK VLHSPPSNVA QNFFETNS
//
