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Database: UniProt
Entry: Q0F3G3_9PROT
LinkDB: Q0F3G3_9PROT
Original site: Q0F3G3_9PROT 
ID   Q0F3G3_9PROT            Unreviewed;       727 AA.
AC   Q0F3G3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=SPV1_04138 {ECO:0000313|EMBL:EAU55978.1};
OS   Mariprofundus ferrooxydans PV-1.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU55978.1, ECO:0000313|Proteomes:UP000005297};
RN   [1] {ECO:0000313|EMBL:EAU55978.1, ECO:0000313|Proteomes:UP000005297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV-1 {ECO:0000313|EMBL:EAU55978.1,
RC   ECO:0000313|Proteomes:UP000005297};
RA   Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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}.
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:EAU55978.1}.
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DR   EMBL; AATS01000001; EAU55978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0F3G3; -.
DR   STRING; 314344.AL013_04240; -.
DR   eggNOG; COG1530; Bacteria.
DR   HOGENOM; CLU_003468_5_3_0; -.
DR   InParanoid; Q0F3G3; -.
DR   OrthoDB; 9804278at2; -.
DR   Proteomes; UP000005297; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   CDD; cd04453; S1_RNase_E; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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:SF1; RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF20833; RNase_E_G_Thio; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005297};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          36..119
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          501..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   727 AA;  81680 MW;  A4BD4D849BD196C2 CRC64;
     MLINASHDEE SRVAIAEDGY LHELDIESAQ KTLTKSNIYK GKVTKVEASL QAAFVEYGAA
     RQGFLSLSEI HPDYWKDGVD KSTNPRNISI QDVLAPKQEL LVQVVKEERG NKGAALTTQI
     SLAGRYLVLS PNTTRGGISR KLSDEERRSM KEILSQLDVP ENMGLIIRTA GKDQTLEALQ
     RDYQYLRRLW DEIRIKSETT PPPALIYLEG DLATRAIRDH FSDDVDEIWV DNHEIYTHTK
     AFVHAVLPGK EKLVKLYRGK IPLFRKYGIE SQCEEMHERE IRLRTGGSIV LDPTEALTSI
     DVNSARATKG KHIDDTALAI NLEAAEEIAR QLRIRDIGGL IVIDFIDMAS RKHGQQVEDM
     LRKACKGDKA RIQFARISRF GLLEMSRQRL HPSVRESTTE PCPRCQGRGF IRTVDSMALQ
     MLTRMEDWAE AGKKPTLVVQ VPSDTGEYLM NNKRDNIARI EETYEIQITL QIRPDLDIPH
     YRIERQWTEN NQQRVEVLED TNKRVKPPRP NRKLKPMKPV VGIPTPPPEL AEKAEEKKKG
     PLTTLIAMLT GQSRKEKLQK EAEEKAQAER EAQRQSERSR NSRARGEKKS RRKPAAAKTS
     APENVAEEKQ KTDSNNPNSE KNTPKKPRRP RKPRAPKPEG EATVNSATEQ QSAEGTTDAP
     KPKRRRRRRP RRPAGNGEAN NNSGQENSAS TGNGGTSEPA ADKPAASRAP ESATTVQAAP
     PSTPQGE
//
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