ID   A0A329ZIW1_9HELI        Unreviewed;       671 AA.
AC   A0A329ZIW1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-NOV-2024, entry version 20.
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=CCY99_01255 {ECO:0000313|EMBL:RAX55353.1};
OS   Helicobacter sp. 16-1353.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=2004996 {ECO:0000313|EMBL:RAX55353.1, ECO:0000313|Proteomes:UP000251728};
RN   [1] {ECO:0000313|EMBL:RAX55353.1, ECO:0000313|Proteomes:UP000251728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16-1353 {ECO:0000313|EMBL:RAX55353.1,
RC   ECO:0000313|Proteomes:UP000251728};
RX   PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA   Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA   Marini R.P., Fox J.G.;
RT   "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT   necrotizing factor (CNF) colonize laboratory macaques.";
RL   Gut Pathog. 9:71-71(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAX55353.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NHYM01000001; RAX55353.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A329ZIW1; -.
DR   OrthoDB; 9770211at2; -.
DR   Proteomes; UP000251728; 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; IPR055132; RNase_J_b_CASP.
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; PF22505; RNase_J_b_CASP; 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|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          138..334
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         483..487
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ   SEQUENCE   671 AA;  76302 MW;  2001A2A247D1A99E CRC64;
     MENNNENTNN QIPEGNKDNK IQNNQPSEKK VFRKWKPKEQ RDKSNKENKN YNRDYKKDST
     EKRFNSYNNS NNQKQDGVSN IQEGLNEKSN LGLHKDLKKI VELNNKSYKN TLNPHYKLDL
     NTRAKIRITP LGGLGEIGGN ITVIESQDSA IIVDAGMSFP EAEMHGVDIL VPDFSYLHAI
     KDKIVGLIIT HAHEDHIGAV PHLFKQLQFP IYGTPLPLGM IGNKFDEYGL KKFRSFFRIV
     EKRKPIKIGD FEVEWIHITH SVIDASALAI KTTAGVILHT GDFKIDHTPV DNFPTDIHRL
     AYYGEHGVML MLSDSTNSHR QGYTPSESSV GPAFENIFKN TQDRIIMSTF SSNIHRVYQA
     ISYGIKFNRK ICVIGRSMEK NLEIARQLGY INIPQNAFID AHEVEKYSDS EILIVTTGAQ
     GEPMSALYRM ATDEHRHIKI KPTDTIIISA KPIPGNENSV SKVINFLMKS GAKVAYQDFS
     EIHVSGHAAQ EEQKLMLRLI KPKFFLPIHG EFNHLAKHRE TAIKCGILEK NILLMEDGDQ
     IEVCPNYVKK IRSVKNGKLF VDNQLGKIID NLTVLDRQKL AEDGIIIIAM QIKNNKIVEN
     PRIQTFGLLG DKEERMFVKE LDDAIKLYVS TAKVESLSKN LEGNLKSHLR KIAFKKFKKY
     PTIVLNIYFL G
//