ID A0A4U8SQY9_9HELI Unreviewed; 709 AA.
AC A0A4U8SQY9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=LS69_000040 {ECO:0000313|EMBL:TLD89071.1};
OS Helicobacter sp. MIT 05-5294.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1548150 {ECO:0000313|EMBL:TLD89071.1, ECO:0000313|Proteomes:UP000029926};
RN [1] {ECO:0000313|EMBL:TLD89071.1, ECO:0000313|Proteomes:UP000029926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 05-5294 {ECO:0000313|EMBL:TLD89071.1,
RC ECO:0000313|Proteomes:UP000029926};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
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:TLD89071.1}.
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DR EMBL; JRPA02000001; TLD89071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8SQY9; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000029926; 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 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 172..368
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517..521
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ SEQUENCE 709 AA; 80017 MW; B940F366601D2826 CRC64;
MEKKEINENQ NPTSQKRVAN PTAKSAEGAS ERSNESQARG EKRENREPNR RHFRPRQPKE
TSENNGADKP RNAQKPQNRK THNPRFKKQE NPQNKPNGET RENPRGNARS NHNKFDKNYG
NKEVNASNLE LRKAVKLNAK VHENALTLHS QVEVNPNGKV RITPLGGLGE IGGNMTIIET
QNSAIIIDAG MSFPDDSMHG VDILVPDFSY LEVIKDKIAG ILITHAHEDH IGAMPYLFKK
YQFPIYGTPL PLGLIGSKFD EHGLKKFRSL FRAVEKRKPI QIGEFEIEWI HITHSIVDSS
ALAIKTEAGL IFHTGDFKID HTPIDGYPTD LNRIAHYGEQ GVLLLLSDST NSHKSGYTPS
EASVGPAFDL LFSRAKGRVI MSTFSSNIHR VYQAINHGLK YGRKVAVIGR SMEKNLEIAR
TLGYIDLPQN IFIEAHEVAK YADEEVLIVT TGSQGETMSA LYRMATDEHR HIKIKPSDTI
ILSAKAIPGN EGSVSNILNF LNKAGAKVYY QDFSEIHTSG HAAQEEQKLM LRLVKPKFFL
PVHGEYNHIL KHKETAISCG VEERNIYLME DGDQMEIAHN YLRKVRSVKT GKTYIDNQVN
STIANDVILD RQNLAENGIL VVHIELSKSK NTLTSKPRIQ SMGIVANKDT MSFNKEIEEF
FTLFVKTCKK ELYNSQKAME NEIRNSLRKL MFRKTKRYPT ILPFVNLVG
//
