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Database: UniProt
Entry: A0A0D2TCD6_9PROT
LinkDB: A0A0D2TCD6_9PROT
Original site: A0A0D2TCD6_9PROT 
ID   A0A0D2TCD6_9PROT        Unreviewed;      1246 AA.
AC   A0A0D2TCD6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 16.
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=N826_00690 {ECO:0000313|EMBL:KJB97341.1};
OS   Skermanella aerolata KACC 11604.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Skermanella.
OX   NCBI_TaxID=1385368 {ECO:0000313|EMBL:KJB97341.1, ECO:0000313|Proteomes:UP000032292};
RN   [1] {ECO:0000313|EMBL:KJB97341.1, ECO:0000313|Proteomes:UP000032292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 11604 {ECO:0000313|Proteomes:UP000032292};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Skermanella aerotala.";
RL   Submitted (AUG-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJB97341.1}.
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DR   EMBL; AVFK01000001; KJB97341.1; -; Genomic_DNA.
DR   EnsemblBacteria; KJB97341; KJB97341; N826_00690.
DR   PATRIC; fig|1385368.3.peg.143; -.
DR   BioCyc; GCF_000936425:N826_RS00680-MONOMER; -.
DR   Proteomes; UP000032292; 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:UP000032292};
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:UP000032292};
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       39     84       S1 motif. {ECO:0000259|Pfam:PF00575}.
FT   REGION       94    376       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   REGION      697    700       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   REGION      829   1059       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   REGION     1092   1246       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   COMPBIAS     94    126       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   COMPBIAS    210    228       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   COMPBIAS    313    357       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   COMPBIAS    873    920       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   COMPBIAS   1040   1056       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   COMPBIAS   1164   1187       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                A0A0D2TCD6}.
FT   METAL       596    596       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       639    639       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       697    697       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       700    700       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   1246 AA;  136517 MW;  F92A97FBD5374876 CRC64;
     MAKRMLIDAT HAEETRVVVV NGNKLDELDF EIASKKQLKG NIYLAKVTRV EPSLQAAFVE
     YGGNRHGFLA FSEIHPDYYR IPVADREALL AQERDLEERE ESAGGDVEMG DPRPGRNQRR
     SFRGGPRGDD NGGAGSHSGQ DRPGQQNEPV AEEPQAGIPG AGEQPPYESG PAGQAPYHEP
     APQPDIGDVP LDWFAPDEPA PEANPPEEPQ SQDGAAQDSG NQDDGQDNGG NAGPDENGDG
     GDKPTTYQPA NLPRDERSEP YEPSDSDAGH PSYDAPRFDA PVEAVIHPVP GSAPAAPAAE
     LGAGTEPAVS EDASIEGGRH RSDSVEDREN TENDHEDDGS RRHRRADRSR NEAEGGSVDD
     LGGDEADDAQ RRRPRPLRSY KIQEVIKRRQ ILLVQVVKEE RGNKGAALTT YLSLPGRYCV
     LMPNTGRGGG ISRKITNPQD RKRLKEMMSD LDIPEGMAVI LRTAGMERTK PEIKRDLEYL
     LRLWDSIRDL TLQSSAPALI YEEANLIKRS IRDLYTNDID EVHVEGENGF RVARDFMHML
     MPSHTRKVQL YRDETIPLFF RYQVETQIDA IHSPVCQLKS GGYIVINQTE ALVAIDVNSG
     RSTRERNIEE TAHKTNLEAA DEIARQLRLR DLAGLIVIDF IDMEDARNNA SVERRIKEAM
     KNDRARIQVG RISPFGLLEL SRQRLRPSLM ETNFEKCPHC AGTGMIRSIE SAALYVLRAI
     EEEGIRKRSS EITVHVATKI ALYILNQKRD ALADIERRYS FRVFLFGDDT LIPPEYRLER
     IKARQAGEEI SPIINTERIF AETDRLLERE AEAEEDDAED VPEPVAEVAE PAAPVAAATA
     TSEQTDERGD RRRRRSRRRR RFDDRPEART DEQGEEDRDE TSEDQAEEGS EDLTPEQIEA
     DASFEDDGEE GDEGEEGENG QAFETDANGL RKKRRRGKRG GRRRGRGRLD GEFDNGYAED
     GEQPSEDGQP APVAVEPASE APPAAAEPVN VPVYIDDLGD PFEDLDLPPL HTPAEPQPES
     QPEPVAQQPT QVEKLEARPV PAPEPAPVPE PEPLPAAAET IEPASIEPAS IEPVTVGEPA
     IPADVVAEVT APEAAPEVPP AKPKAKRAPR KKKVVEPAAE AAPAPVVAEP APEAPAAKPK
     AKRAPRKKKV VEPAAEAAPA PVAAEPAPAE PAPSEQIPEP VPAPLPQEPS AGDDLFMDVA
     PGPVEPAPEP DLPPESEQAA EPAAENQEDS ESQPAAPPRR GWWSRG
//
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