ID A0A0G4GIA3_VITBC Unreviewed; 1005 AA.
AC A0A0G4GIA3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Vbra_17834 {ECO:0000313|EMBL:CEM29576.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM29576.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM29576.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
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DR EMBL; CDMY01000677; CEM29576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4GIA3; -.
DR STRING; 1169540.A0A0G4GIA3; -.
DR VEuPathDB; CryptoDB:Vbra_17834; -.
DR InParanoid; A0A0G4GIA3; -.
DR OrthoDB; 937144at2759; -.
DR Proteomes; UP000041254; 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 CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR CDD; cd00164; S1_like; 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; 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; 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; 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; 2.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1005
FT /note="polyribonucleotide nucleotidyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005190523"
FT DOMAIN 732..803
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 847..918
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 61..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 109141 MW; 27BC7B439744B02B CRC64;
MKPMGSSSWR LVHFVCALGA LVDLASALRR GSGDAAGFAH PLVSEGLQRL QQPLTSRLRS
APFSVSTDVS PESVQSHDDA TTESDLPFSV PHSEPGESYW EVLPSAAQTV HRQTIEKYGD
YDVILETGNV ARQAAGSVMV RMGDCVVLSA VTVSERDTDK DFFPLRVDYV EKVYSAGRIP
GGWTKREMSQ QDPEILIGRL IDRPIRPLFP KWFKREVQIV TTLLSYDENV DPAIPALLGA
SAALTLAGVP FQRPLGAARV GYVDGEYVLN PTAAEDDISG LDLTVAGTSE AIMMVEAQAN
ELTEEVVLGG ILYGHEQARR AIEAIQQLAD KAGRNTAFTQ MTPPPDQESR RLPLGLDATI
DHLADAIVRT GDKGGRAELT KDAEAQLRAA CDDPEMMHVV TGMLESRVKE RMRQRVLSEG
VRVDGRGLKE VRSIACSVGL LPRVHGSALF TRGGTQSLST VTLGGDRDAK QIDDVRSDRL
PFILHYNFPP YSVNEIGFLG RPKRRDIGHG WLARRALQTL MPSEFAFPYT VRVVSEITES
DGSSSMATVC ASSLALMDAG VPLSKPVAGV AMGLIKDPNG PLFAVLTDIM GFEDALGDMD
FKVAGTTEGI TALQMDIKIG GIDGSVLKEA LAQAREGRMH ILNEMSATIA EPRTSLSPWA
PQIFTHQIKP SQMGDVIGRG GERVRQLEED YSVKITVSDD GLVQILAEDP RKGREVLEYI
KGITDETPIP LGTRFDNAQV VQVAPAFVIV KLNEFREGFL HVSETPEGDS FVPNLGAVYP
VGNNLTVWVK EVQENGRLRV TAREETGALL EQAQGSEEEI QKLLSELQTK KGAGARQAPI
RIDYKVGDEV KGAMVDRIFP KHAILKLPGA DRAGLLPIGK IANEYVPNVR DYFKEGQEVR
VWVDDLAPGK RSIIVTAIPP PPDSTPDGHD DYEKAPTPSP LFELRSGSLD SLLDEAYADL
ERSKSQGAKP RRDKGGGRGK PRLAPVDTLV GEGGGEEGNQ QDVKR
//
