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Database: UniProt
Entry: A0A0B6WZH6_9BACT
LinkDB: A0A0B6WZH6_9BACT
Original site: A0A0B6WZH6_9BACT 
ID   A0A0B6WZH6_9BACT        Unreviewed;       777 AA.
AC   A0A0B6WZH6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=PYK22_02102 {ECO:0000313|EMBL:CDM66092.1};
OS   Pyrinomonas methylaliphatogenes.
OC   Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC   Pyrinomonadaceae; Pyrinomonas.
OX   NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM66092.1, ECO:0000313|Proteomes:UP000031518};
RN   [1] {ECO:0000313|EMBL:CDM66092.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66092.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Stott M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDM66092.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66092.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA   Stott M.B.;
RT   "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT   K22T.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC       {ECO:0000256|ARBA:ARBA00005663}.
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DR   EMBL; CBXV010000007; CDM66092.1; -; Genomic_DNA.
DR   RefSeq; WP_041976962.1; NZ_CBXV010000007.1.
DR   AlphaFoldDB; A0A0B6WZH6; -.
DR   STRING; 454194.PYK22_02102; -.
DR   OrthoDB; 9804278at2; -.
DR   Proteomes; UP000031518; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR   Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR048583; RNase_E_G_thioredoxin-like.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00757; RNaseEG; 1.
DR   PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR   PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF20833; RNase_E_G_Thio; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDM66092.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          40..94
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          82..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  87315 MW;  27C3A976136CFFBF CRC64;
     MPKEMIISVN GREKKIAIIE DGQVTEFYIE RGEANQGVAG NIYKGRVMRV LPGMQSAFVD
     IGLERDAFLY VSDFFDEEEE YERIKVPTGE SARATESPQS RRSAPTEERP QDLLTEATPS
     PIELAEDEGS PLASPSAEEA SPEPKTEELR PVEDLTTPFV AESSFERILD EEVAAEEGEL
     FKDAILQERL SDEVRAIEFD IEPTSTAEVG SILPSSTPSP SGLERVDDIE PEAQSHEERT
     PPSLASEVQP VENETQPRRR SRSKKAAGET EETASKRRGR SKSGASEQTS TARRKRRKAE
     AEGSETQLED REARLSSSRS RAEFARRRRR RRAKQQPETP AETSNGNGAD AAAEVAEALP
     GRADGSRHPH PSITELLREG QEILVQIAKE PIGQKGARIT SHIALPGRYL VYMPTIEHIG
     VSRKIESANE RARLRKLIQT IMQEEDVPSG GFIVRTAGTG VSEAALREDA RYLIRTWLDI
     RRTAERVKAP ALIHRDLDLV QRILRDQLSD EFTAIRVDSE EEYLRIVEFV NRIQPRLVNR
     VKLYTRDEPI LEAYGVQQEI DKAIKPRVWL KSGGYLVINQ TEALVAIDVN TGKFVGRGSN
     RLEDTITKTN LEAVEEIARQ IRLRDLGGII VLDLIDMEER RNRQRVLQAL QEALQHDKSP
     TKVLSYNDFG LVIMTRKRVK QSLERTLCSP CPYCQGAGLV KSPQTICYEI LEEARRLARS
     MNGEPIKQVT LRVNPEVARA LRTTERDVLA EVEEYLGAVD ITSDESVHQE QFDFAFV
//
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