ID V8CBC6_9HELI Unreviewed; 699 AA.
AC V8CBC6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=HMPREF2086_00046 {ECO:0000313|EMBL:ETD24713.1};
OS Helicobacter macacae MIT 99-5501.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD24713.1, ECO:0000313|Proteomes:UP000018731};
RN [1] {ECO:0000313|EMBL:ETD24713.1, ECO:0000313|Proteomes:UP000018731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD24713.1,
RC ECO:0000313|Proteomes:UP000018731};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(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:ETD24713.1}.
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DR EMBL; AZJI01000001; ETD24713.1; -; Genomic_DNA.
DR RefSeq; WP_023926715.1; NZ_KI669454.1.
DR AlphaFoldDB; V8CBC6; -.
DR STRING; 1357400.HMPREF2086_00046; -.
DR PATRIC; fig|1357400.3.peg.69; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_0_7; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000018731; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000018731};
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 164..360
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 618..645
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 44..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..513
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ SEQUENCE 699 AA; 78130 MW; BA27346F1FDBF4D7 CRC64;
MNDNNEQQKR GFFSRFGKKD GQSPQNNHNS HNKDHRNHKN KHRQNGGQNS TTNEANSSQR
DSSQNGQNSQ NNAKHQNQPN SAAPQKRQFP NQRMQALQDS ASRGAREVQG AKEKGNLEFH
KDLKKGVETN TRIQKNSLNP HNKLDLSTKE KIKITPLGGL GEIGGNMMVM ESENSAIIID
VGMSFPEENM HGVDILIPDF SYLHSIKSKI AGIVITHAHE DHIGAVPYLF KELQFPLYGT
PLALGMIGAK FDEHGLKQYR PMLKVVQKRQ PVQIGDFEIE WIHITHSIID SSALGIRTAA
GIILHTGDFK IDHTPIDNLP TDLHRLAHYG EEGVMLLLSD STNSHKSGCT QSEATVGPTF
DALFKNADGR VIMSTFSSNI HRVYQAITYG LKYGRKVCVI GRSMEKNIEI ARELGYIDLP
NNIFIEAHEV EKYPDSEILI VTTGSQGETM SALYRMATDE HRHIKIKSSD LIILSAKAIP
GNEGSVSAVL NFLMKAGASV AYQDFSEIHV SGHAAQEEQK LMLRLIKPKF FLPVHGEYNH
VSKHKDTAIK CGVPEKNILL MEDGDQIEVN PTYIKKVGNV KSGKVFIDNQ ACKEIDAPTL
QDRKDLADSG IVSVVAFIAK QEQKLRSLEI QMVGVANQNE QKELEKEVQG TIEMAIRTIK
KETMNSKGHL EAELRNIIRK LLFKKLKKYP AIMMHIFTA
//
