ID A0A2P6V2R8_9CHLO Unreviewed; 1063 AA.
AC A0A2P6V2R8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, 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 ORFNames=C2E20_8069 {ECO:0000313|EMBL:PSC68371.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC68371.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC68371.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC68371.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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:PSC68371.1}.
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DR EMBL; LHPF02000038; PSC68371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6V2R8; -.
DR STRING; 554055.A0A2P6V2R8; -.
DR Proteomes; UP000239649; 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; cd22271; DPBB_EXP_N-like; 1.
DR CDD; cd02393; KH-I_PNPase; 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 Gene3D; 2.40.40.10; RlpA-like domain; 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; IPR036908; RlpA-like_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 Pfam; PF00575; S1; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 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:UP000239649};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PSC68371.1}.
FT DOMAIN 801..869
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 883..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 111215 MW; 18810E3073B4FDB4 CRC64;
MSGRATALRR CATLLARGCQ AQLEREAGAA AAACELGLSS TGRGTAATTL PAVAQRFSTA
SPARLHSATP QAPADAPLRE ASLVRDDIGD ALRGEAEAFP LSDEEAAAAA ASAAAADAAL
ERLAGQHLVP TDAIATLPRG QSLRQEGEFQ GQSWAFETGK MARLANGSCM VQAGGTSVLA
AATAQAAPWS RRDAYQLQFE VEYREKLCAV GRIPSTYNKR EGAAKEHEVL AARRIDRALR
PLFPRGLPFD AALFANVLSA DGSADPDVMA ISAASAALMC SDLPWAGPVA AARVAVLPGG
ELVVGPSVAQ QEAAALTLLV AATAERVTML EAEGAQIPEA EFMRALRAGV EAAQALVEPQ
RLLAEQTGRS TRTVQLSGAD PAAARRVTEM VAPAVEAILR NAELSKSARI QALQEAKEAV
LQKLRASGGF RADFARVPGS GCVTQADLEH TFRALVAGTL RRLALDEGWR CDGRGGIDVR
SVHCEVDVVP VVHGSALFSR GETQSLCTAT VGRRGEQQKT ESLMGGEGYK RIFVNYSFPA
YAVGETSIGG MRREWGHSEL CERALLPVLP AENEFPFSLR INAETLASAG SSSMAAVSGG
ALALADAGVP LKALVAGISV GLFMDDSWDG ACGELAGAPV AQAGGAAVPP VGRYELLTDL
QGIEDQTGGM DLKVAGTRTG ITACQLDVKL PGGVPLSIVE EALAAAARGR AKILSAMEAA
LPEERSDSSP TFGSLTVPAG MVGRVIGSGG SNIRQLEEEA DVRLDVDGDS GRVAIYAPSQ
AAYKLAASKV QDVTGESVKE GEVYRGTVTK LFDYGALVTL ADSGARALLH ISEISPTRVR
SIEEALSLGQ ELEVMCLGRD ARGMRLSRKA VLARADAQAR SAEQVQHSGG VDADNPGHSS
SLSSLPSPPL IMASLRSSLA LALVLCVAGA SAYYKGDGTA YSGKGNKNHT GFNSCQFGTL
DSKWETLYAA LPSQVFNKDE DCGKCIKVRG TEPDAPGKWV TIMVVDECAS CEGDGDVDFS
DVALEKITGY NWDRKGIEWD WVDCEEETKQ ALSTQKSRKM LHA
//
