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Database: UniProt
Entry: A0A1I6QVI5_9RHOB
LinkDB: A0A1I6QVI5_9RHOB
Original site: A0A1I6QVI5_9RHOB 
ID   A0A1I6QVI5_9RHOB        Unreviewed;       989 AA.
AC   A0A1I6QVI5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 6.
DE   RecName: Full=Ribonuclease E {ECO:0000256|HAMAP-Rule:MF_00970};
DE            Short=RNase E {ECO:0000256|HAMAP-Rule:MF_00970};
DE            EC=3.1.26.12 {ECO:0000256|HAMAP-Rule:MF_00970};
GN   Name=rne {ECO:0000256|HAMAP-Rule:MF_00970};
GN   ORFNames=SAMN04488040_0973 {ECO:0000313|EMBL:SFS56380.1};
OS   Sulfitobacter marinus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=394264 {ECO:0000313|EMBL:SFS56380.1, ECO:0000313|Proteomes:UP000199239};
RN   [1] {ECO:0000313|EMBL:SFS56380.1, ECO:0000313|Proteomes:UP000199239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23422 {ECO:0000313|EMBL:SFS56380.1,
RC   ECO:0000313|Proteomes:UP000199239};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that plays a central role in RNA
CC       processing and decay. Required for the maturation of 5S and 16S
CC       rRNAs and the majority of tRNAs. Also involved in the degradation
CC       of most mRNAs. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and
CC         U-rich regions.; EC=3.1.26.12; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- SUBUNIT: Homotetramer formed by a dimer of dimers.
CC       {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}.
CC       Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic
CC       side {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00970}.
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DR   EMBL; FPAJ01000001; SFS56380.1; -; Genomic_DNA.
DR   Proteomes; UP000199239; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00970; RNase_E; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR028878; RNase_E.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF00575; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00757; RNaseEG; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199239};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199239};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   DOMAIN      104    144       S1 motif. {ECO:0000259|Pfam:PF00575}.
FT   REGION        1     30       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   REGION      163    292       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   REGION      612    615       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   REGION      724    989       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS      1     28       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    163    208       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    220    234       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    235    256       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    257    273       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    742    761       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    779    797       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    798    837       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    867    912       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   COMPBIAS    913    940       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A1I6QVI5}.
FT   METAL       511    511       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       554    554       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       612    612       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       615    615       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   989 AA;  109420 MW;  6A59362FCA053BA5 CRC64;
     MDVNRAKVPF TSEKNRDDAR RRHEQTNRRP FGPCFSRVTY RPDKTYPAAR CPTRTPACAA
     VQNGFMPKKM LIDATHAEET RVVVVDGNKV EEFDFESENK RQLAGNIYLA KVTRVEPSLQ
     AAFVDYGGNR HGFLAFSEIH PDYYQIPVAD RIALMEEERA YAEAQAAKDE DDEKPKRRTR
     SRSRSKAKAE DTVSEDAVAT KDADSDQIDG METVDLDDEE GSSPMERVAE TPVEEPDQDE
     ASSDADDSDA DVDGDDDEPE AKAKDASSKD DSIESVADDD DQEDLRPARK PRPKRYKIQE
     VVKVRQILLI QVVKEERGNK GAALTTYLSL AGRYCVLMPN TARGGGISRK ITNAADRKKL
     KEIANEIQVP KGAGLIVRTA GAQRTKAEIK RDYEYLQRLW EQIRELTLKS IAPAKIYEEG
     DLIKRSIRDL YNRDIDEVFV EGERGYRIAK DFMKMIMPSH AKNVKLYSDS LPLFARYQVE
     SYLSGMFNPT VQLPSGGYIV IGVTEALVAI DVNSGRATKE GSIEQTATKT NLEAAAEVAR
     QLRLRDLAGL IVIDFIDMDE RRNNIAVEKM MKDKLKTDRA RIQVGRISGF GLMEMSRQRL
     RPGMIEATTQ PCHVCHGTGL IRSDDNLALS ILREIEEEGT RKRSREVLVT APVGIANFLM
     NQKREHIAHI EGRYGMSVRI EGDPTLVSPD FKIEKFKTAT RVVAQIEHVV SVDTSLMDEI
     DEQEAETVDA DEGANEDQPA NRGNGRAHDN DGEDNEGEGK PKRRRRRRRR RGGKSNGDDA
     ANGENNGAES ATSDDNQPAE AKPDDSDAGA KADDAAEKTA DADATEAKPE AAEKPKRTRR
     PRKPKADVAA EADSADATVS AEATDAAEEA AEEKPTPKKR TRTRKPKVAE EDKADGKSDD
     KPEKKPARKS KPKPEPTPVP APEPAPVEPT PAPVEVPIEA PVEVPPTQEV APAPAVEEVP
     DQTAAPAPEK VEGKPAKPRR RGWWSLGGS
//
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