ID F5Z8Y9_ALTNA Unreviewed; 1100 AA.
AC F5Z8Y9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=ambt_10030 {ECO:0000313|EMBL:AEF03532.1};
OS Alteromonas naphthalenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF03532.1, ECO:0000313|Proteomes:UP000000683};
RN [1] {ECO:0000313|EMBL:AEF03532.1, ECO:0000313|Proteomes:UP000000683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC {ECO:0000313|Proteomes:UP000000683};
RX PubMed=21705606; DOI=10.1128/JB.05252-11;
RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA Oh T.K., Kim J.F.;
RT "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT bacterium Alteromonas sp. strain SN2.";
RL J. Bacteriol. 193:4292-4293(2011).
CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA processing
CC and decay. Required for the maturation of 5S and 16S rRNAs and the
CC majority of tRNAs. Also involved in the degradation of most mRNAs.
CC {ECO:0000256|HAMAP-Rule:MF_00970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-
CC 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;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00970};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00970};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00970};
CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP-
CC Rule:MF_00970};
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation. Within the RNA
CC degradosome, RNase E assembles into a homotetramer formed by a dimer of
CC dimers. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}. Cell
CC inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral membrane
CC protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic side
CC {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 -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000256|ARBA:ARBA00005663}.
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DR EMBL; CP002339; AEF03532.1; -; Genomic_DNA.
DR AlphaFoldDB; F5Z8Y9; -.
DR KEGG; alt:ambt_10030; -.
DR eggNOG; COG1530; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_003468_1_3_6; -.
DR Proteomes; UP000000683; Chromosome.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 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 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; 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, ECO:0000256|HAMAP-
KW Rule:MF_00970};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00970}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00970};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00970};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00970};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00970}; Nuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00970}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00970}.
FT DOMAIN 39..119
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 403..406
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT REGION 569..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
SQ SEQUENCE 1100 AA; 120253 MW; A92CF346801964B8 CRC64;
MKRMLINATQ LEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRVE PSLEAAFVDY
GADRHGFLPL KEIARTYFPK GYRFEGRPNI KDVIKEGQEV IIQIDKEERG QKGAALTTFL
SLAGSYLVLM PNNPRAGGIS RRIEGDERTE LKESLNKLDL PDGMGLIVRT AGVGKSYEEL
EWDLKVLLTH WEAISKVAEE REAPFLIHQE SNVIVRAIRD YLRRDIGEIL IDKTSIYEQA
LQHIQLVRPD FASRVKLYRG EVPLFSHYQI ESQIESAFQR EVRLPSGGSI VIDPTEALTS
IDINSARATK GGDIEETALN TNLEAADEIA RQLRLRDLGG LVVIDFIDMT PVRHQREVEN
RMKDAVRSDR ARVQLGRISR FGLLEMSRQR LRPSLGDSAH HVCPRCSGHG TIRGTESLAL
SILRILEEES IKENTGQIEA QLPVSVATYL LNEKRKAIQS LEKRHGVNLL LIPNANLETP
HYQVTRRRPD DILDDASYEV ELMPTVETET ETTTSVPVKR EEPALKGLVA PTAAPVVAPK
AETPEAKAES SPSLFARIGK WLGDVLGGED EKAKAEAEAK EKEKQKQSES RNNRGGNQSR
NRNGDDRRRK PRKNTRRNQP QNKDGEQEQR TPRSEQDDKP RASNNKPRKP RKPRDETQKP
KQDQSRDNAQ DEAPKTQDRK SQDAKPQEAQ KKQEVAERRK RRDTRRSVRV KKDDNTQSNE
APASKPVKSL AVDKPKPAKA APAETEEVNT SPVQSTDAPA ASESAAPVTQ ASQPADVKST
TEQDAQSSSE QSNNDTDENG QKRESRGRSR RSPRHVRAAG QRRKKEAQQS NDDNSAPVGE
QSTTNVETTP SQEVPASTAP AADVSESAPR AEDTQAAMPG KLEADTAHTQ NENAQPAAID
ASADNAEAPT ATKAEDTQAT KPSVLAPSEE KAEPATTETA SAKPEAPAAE VVQDEMQFEL
ASPKSEADAP KPAKADVTPA PVAEAAPKQV EINLGEDSAK AASEPKAKPA PKANLKKAKA
AVSKPITTGV AASSRGRINA SAPMAAPASV DDTFNDVALT AKSDDSRPAI VVSGRSAAIA
KASAAASAPT TLPSSVDENA
//
