ID A0A0V1D0Z6_TRIBR Unreviewed; 763 AA.
AC A0A0V1D0Z6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=PNPT1 {ECO:0000313|EMBL:KRY55112.1};
GN ORFNames=T03_16982 {ECO:0000313|EMBL:KRY55112.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55112.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY55112.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY55112.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY55112.1}.
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DR EMBL; JYDI01000060; KRY55112.1; -; Genomic_DNA.
DR EMBL; JYDI01000060; KRY55113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D0Z6; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
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; 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; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 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:UP000054653};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY55112.1}.
FT DOMAIN 676..747
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 763 AA; 82613 MW; 1E5AF8262FFCCDF9 CRC64;
MGFFCVVTRL TKFAPFSPLL TSSRPVVSVQ ADVGSVPMIL ETGQLARLAD GSAVAKMGAT
TVMATVVAKS RSAVQPMMFM PLTVDYRSRA AAVGRIPTNF LRREIGASDS EILTARMIDR
SLRPAFGRDC YVDCQVSCSL LSLEADATGA DVLAVNAASA ALACSNVVWN GPVACARVCW
VDSRPVLNPS RQQLEMSTLN LVLSVGEHRR IVMVEAGGGS SGSCSLDQLY ACCDLAVDSA
QRTLDAIKQL AARAGKPKRV PSGQLLPADK PDDLTGAIQL YASATLGELL LDKDLDKMAF
DERVANLRHD TADNLRQADC FQDDQLRFFD VAFNDLLKKA LRDQVFNTGH RRDGRTLDEL
RPIDCSVDLY PSLHGSALFQ RGQTQVMCSL TFDSRQAAFR GDMFSLLNSG GITKEKKFMF
HYNFASFATN ELSSARGIGR RELGHGALAE KALRPVVPSD FPFTIRLAAD VLESNGSSSM
ASVCAGSLAL MDAGVPTKSS VSGVAIGLMS KQDENGNISD YRLLTDIAGI EDFFGDMDFK
IAFTSNGEVT AIQLDTKLLG GIDQRIFRQA CERGLQANRN VQRKMAACLA KPRAAIKPNG
PVEEQLPVPA SKRSRLLGAG GLNLKRIEAR TGVQISQLDD TVYSVFAPNK QAMQQARQSL
DQLLADNVEE EQLEFGAIYE TKIVELKDTG LMVQLHPSLA PVFVPNSQLD SRRIAHPATL
GFQVGQTLLV KYFGRDPVTG QMRLSRKVLQ QIGPAGTKKL GIE
//
