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Database: UniProt
Entry: A0A143Z4Y4_9LACT
LinkDB: A0A143Z4Y4_9LACT
Original site: A0A143Z4Y4_9LACT 
ID   A0A143Z4Y4_9LACT        Unreviewed;       558 AA.
AC   A0A143Z4Y4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491};
GN   Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN   ORFNames=TR210_2176 {ECO:0000313|EMBL:CZR04974.1};
OS   Trichococcus ilyis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Trichococcus.
OX   NCBI_TaxID=640938 {ECO:0000313|EMBL:CZR04974.1, ECO:0000313|Proteomes:UP000076878};
RN   [1] {ECO:0000313|EMBL:CZR04974.1, ECO:0000313|Proteomes:UP000076878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZR04974.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC       activity. Involved in maturation of rRNA and in some organisms also
CC       mRNA maturation and/or decay. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC       {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
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DR   EMBL; FJNB01000017; CZR04974.1; -; Genomic_DNA.
DR   RefSeq; WP_068623706.1; NZ_FNYT01000014.1.
DR   AlphaFoldDB; A0A143Z4Y4; -.
DR   STRING; 640938.TR210_2176; -.
DR   OrthoDB; 9758375at2; -.
DR   Proteomes; UP000076878; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd07714; RNaseJ_MBL-fold; 1.
DR   Gene3D; 3.10.20.580; -; 1.
DR   Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   HAMAP; MF_01491; RNase_J_bact; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   InterPro; IPR004613; RNase_J.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR030854; RNase_J_bac.
DR   InterPro; IPR041636; RNase_J_C.
DR   InterPro; IPR001587; RNase_J_CS.
DR   NCBIfam; TIGR00649; MG423; 1.
DR   PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR   PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   Pfam; PF17770; RNase_J_C; 1.
DR   PIRSF; PIRSF004803; RnjA; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS01292; UPF0036; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01491};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01491};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01491}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          22..217
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   BINDING         366..370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT                   ECO:0000256|PIRSR:PIRSR004803-2"
SQ   SEQUENCE   558 AA;  61121 MW;  50A49D770C57BEE3 CRC64;
     MKPNIKNNEV GVFALGGLGE IGKNMYGIQF QDEIIILDSG IMFPEDDLLG IDYVIPDYSY
     LVQNQTKIKG LFISHGHEDH IGGVPFLLKE LNIPIYAGKL ALAMIRNKLD EHGLLRDAVL
     HEINEDSVIK FRKTSISFFG TTHSIPDTLG IVVKTPPGNI VFTGDFKFDF TPANGKPANI
     HKMAKIGEEG VLLLLSDSTN AETPAFTQSE QIVGQSLKNI IQKVSGRIIF ASFSSNIYRL
     QQVTEVALET GRKIAVFGRS METNFRTARE LGFIVAPDDL FIDARELNSL PADKVLIMCT
     GSQGEPMAAL SRIANGTHRQ ISIQPGDTVI FSSSPIPGNT TSVNRVINQL LEAGAAVVHG
     KVNNVHTSGH GGQQEQKLML TLMKPKYFMP VHGEYRMLKI HTSLAESVGI PAENCFISGN
     GEILALTADS ARRAGNFNAA DVYVDGKGIG DIGNIVLRDR RVLSEDGLVV VVLTVDYRNK
     NLLAGPDILS RGFIYMRESG DLIHEAQTIV RHDVLSLLKS SDSVTEKKLK DTVTNAIQPY
     LYEKTERRPM IVPVIMGV
//
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