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Database: UniProt
Entry: A0A139P662_9STRE
LinkDB: A0A139P662_9STRE
Original site: A0A139P662_9STRE 
ID   A0A139P662_9STRE        Unreviewed;       436 AA.
AC   A0A139P662;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE            EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
GN   ORFNames=STRDD11_01411 {ECO:0000313|EMBL:KXT83632.1};
OS   Streptococcus sp. DD11.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777879 {ECO:0000313|EMBL:KXT83632.1, ECO:0000313|Proteomes:UP000070514};
RN   [1] {ECO:0000313|EMBL:KXT83632.1, ECO:0000313|Proteomes:UP000070514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD11 {ECO:0000313|EMBL:KXT83632.1,
RC   ECO:0000313|Proteomes:UP000070514};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) 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:KXT83632.1}.
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DR   EMBL; LQRF01000168; KXT83632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139P662; -.
DR   STRING; 1777879.STRDD11_01411; -.
DR   PATRIC; fig|1777879.3.peg.1570; -.
DR   Proteomes; UP000070514; 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   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
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; 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; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
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; SSF55666; Ribonuclease PH domain 2-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:KXT83632.1};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00117};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXT83632.1}.
FT   DOMAIN          330..398
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          396..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  47814 MW;  6AB8A2F0C5158229 CRC64;
     MAEILERMEH AEVRRLITED KVRPDGRKVD EIRPLDAEVD YLPRVHGSGL FTRGQTQALS
     VLTLAPMGET QIVDGLDPEY KKRFMHHYNF PQYSVGETGR YGAPGRREIG HGALGERALE
     QVLPSLEDFP YAIRLVAEVL ESNGSSSQAS ICAGTLALMA GGVPIKAPVA GIAMGLISDG
     SNYTVLTDIQ GLEDHFGDMD FKVAGTREGI TALQMDIKIA GITAEILTEA LAQAKKARFE
     ILDLIEATIP APRPELAPTA PKIDTIKIDV DKIKIVIGKG GETIDKIIAE TGVKIDIDDE
     GNVAIYSSDQ DAINRAKEII AALVREAKVD EVYHAKVVRI EKFGAFVNLF DKTDALVHIS
     EMAWTRTNNV EDLVQIGDEV DVKVIKIDAK GRVDASMKVL LPRPPKSDKP RKHHDKPHHP
     KAHKEQQETK AEKPEG
//
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