ID A0A164Z4R3_9SYNE Unreviewed; 668 AA.
AC A0A164Z4R3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=FLM9_794 {ECO:0000313|EMBL:SAY38813.1};
OS Candidatus Synechococcus spongiarum.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=431041 {ECO:0000313|EMBL:SAY38813.1, ECO:0000313|Proteomes:UP000182631};
RN [1] {ECO:0000313|Proteomes:UP000182631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA liu f.;
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; FITM01000090; SAY38813.1; -; Genomic_DNA.
DR RefSeq; WP_074457312.1; NZ_FITM01000090.1.
DR AlphaFoldDB; A0A164Z4R3; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000182631; 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 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|HAMAP-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 Reference proteome {ECO:0000313|Proteomes:UP000182631};
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 24..221
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 571..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 370..374
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ SEQUENCE 668 AA; 73253 MW; 138976B558790B8D CRC64;
MTQTPNGSVE PLRVIPLGGL HEIGKNTCVF EYGNELMLVD AGLSFPSDDM HGVNVVMPDT
TYLRENQHRI RGMIVTHGHE DHIGGIAHHL KHFTIPVIYG PRLALSLLND KMKEAGVSDR
TNTKTVRPRD VVKVGKHFRV EFIRNTHSIA DSFSLAITTP VGVVIFTGDF KFDHTPVDGE
RFDLHRLAQY GENGVLCLFS DSTNAELPGF TPPERAVFPN LDLHIAQAQG RVLVTTFASS
VHRVSMILEL ALKHGRRVGL LGRSMLNVIA KARELGYVRC PDHLFLPMKQ LRDLPDRELL
LLMTGSQGEH LAALSRIARA EHPHVQLKTT DTVIFSASPI PGNTISVVNV IDQLMMQGAT
VIYGKDKGIH VSGHGSQEDE KLMLALARPR FFVPVHGEHR MLVQHCKTAR SMGMPPESML
VIDNGDVVEL TPESIRRGEP VKAGIELLDS SRKGIINTQV LKERQQLAED GVLVVHVSVS
PAGHMGAPAR VTLRGVATSL APQHFADWTD TEVQWALDNR WQQLCRGGDD LQDVDWVGLQ
REVELGLQRR LRRELEVEPL IVVVVQPTPK GSSAIYKAPT TEERGRAGRG SGRPNGVRPL
QRNGGANGHS KNPALVDHRH LSSNGAMTPQ STSPSTLADS GPAVNANGVG PAVEMERKRR
SRSRTGTG
//
