ID A0A067L569_JATCU Unreviewed; 843 AA.
AC A0A067L569;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=JCGZ_02665 {ECO:0000313|EMBL:KDP39645.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP39645.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP39645.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP39645.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; KK914347; KDP39645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067L569; -.
DR STRING; 180498.A0A067L569; -.
DR Proteomes; UP000027138; 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; cd02393; KH-I_PNPase; 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 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; 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:SF17; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 2.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 648..717
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 717..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 91316 MW; C308D0F3F051E717 CRC64;
MVTDGETIVY TTVCLDDIPS EPSDFFPLSV NYQERFSAAG RTSGGFFKRE GRAKDHEVLT
CRLIDRPLRP TMPKGFYHET QILSWVLSYD GLHSPDSLAV TAAGIAVALS EVPTTQAIAG
VRVGLVGDRF IVNPTTKEME ESELDLLLAG TDSAILMIEG YCDFLPEEKL LEAVQVGQDA
VRAICNEVES LVKKCGKPKM LDAIKLPPPE LFKHVEEIAG DEILNVLQIR NKIPRRKALT
SLEEKVIGIL TEKGYVSKDI SFGTTETVAD LLEEEDEDEE VVVDGEVDEG DVHIKPISRK
SSPLLYSEVD VKLVFKEVTS KFLRRRIVEG GKRSDGRMPD GIRPINSRCG LLPRAHGSVL
FTRGETQSLA VVTLGDKQMA QRVDNLVDVD EFKRFYLQYS FPPSCVGEVG RIGAPSRREI
GHGTLAERAL EPILPSEDDF PYTIRVESTI TESNGSSSMA SVCGGCLALQ DAGVPVKCSI
AGIAMGMVLD TEEFGGDGTP LILSDITGSE DASGDMDFKV AGNEDGVTAF QMDIKVGGIT
LSAMKKALLQ AKDGRKHILA EMLKCSPPPS KRLSKYAPLI HVMKVHPEKV NMIIGSGGKK
VRSIIEETGV ESIDADEDGI VKITAKDLSS LEKSKSIISN LTMVPTIGDI FRNCEIKSVA
PYGVFVEIAP GREGLCHVSE LTSSWLPKAE DAFKVGDRVD VKLIEVNDKG QLRLSRKALL
PEPAVEKPSA KQETDDPNKS TSVSQKATDK GNAKRTVSSP KDGLTEGTIE KPEDKTGAPE
VVTSPKSNTL EDSSVPKKKV YRRLASSARD GPNIKKDLLQ KSSSEVATGI ATEDGSTIVN
GEA
//
