ID A0A117M4B9_9BACT Unreviewed; 621 AA.
AC A0A117M4B9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE Flags: Fragment;
GN ORFNames=XD98_0299 {ECO:0000313|EMBL:KUK83602.1};
OS Microgenomates bacterium 39_6.
OC Bacteria; Candidatus Microgenomates.
OX NCBI_TaxID=1641391 {ECO:0000313|EMBL:KUK83602.1, ECO:0000313|Proteomes:UP000053541};
RN [1] {ECO:0000313|Proteomes:UP000053541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK83602.1}.
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DR EMBL; LGGT01000035; KUK83602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117M4B9; -.
DR PATRIC; fig|1641391.3.peg.277; -.
DR Proteomes; UP000053541; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
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; PF03726; PNPase; 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; 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; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUK83602.1}.
FT DOMAIN 503..571
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 572..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK83602.1"
SQ SEQUENCE 621 AA; 67698 MW; 98F266263AB9DA66 CRC64;
VLSVDGQNDP VLLGAIASFS ALTFSSAPWQ GPLGIVGVGQ DEKGELILNP TTDQKEKSSL
DLIVAGTAQR VVMIEAEGKQ VKEEIADSAI DFAMKGNGKL IDFIVDMGKE AGKDKVAFKP
TENKALEKEV SSFVSKDLST IFEKNGDCLD YLSTIKETAI NHFQDDDPKE IDKIIEKLFK
KAIKKRLLKG IRPDGRKTDE VRPISVEIGL LPRTHGSSLF KRGKTHVLNI ATLGPLSLGQ
TIESAEGEEE KRYIHHYSMP PFTVGEAGFM RGPGRREIGH GALAEKALLP VIPSEEDFPY
AILLVSEVMS SDGSTSMASV CSSSLSLMDA GVPISDAVAG IAIGIVTDKK GDKEEYQLLT
DIAGIEDFNG EMDFKVAGTD KGITAIQLDV KNKGLTSQMV TETLAAAKKA RGEILSVMNK
AIDKSRKNLS QWAPKVDVIT VDKEKIGEII GPGGRMIKQI SKETDCEINV EDDGKVSIIG
HDRESIKKAL DWIEGLVREV EPGEVFEGTV ERIESFGAFV NILPNRDGLV HISNMASGYV
KDPRDVVSIG DKVKVKVIKV DERDRVNLTM VLDDNDSSGE NSQNKSSSKK TDSGKERSNS
HGRKKLKKTA EFDRFSHFRK R
//
