ID   A0A5L4RW15_CAMUP        Unreviewed;       676 AA.
AC   A0A5L4RW15;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   12-AUG-2020, entry version 4.
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=CJO62_04210 {ECO:0000313|EMBL:EAK1340513.1};
OS   Campylobacter upsaliensis.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=28080 {ECO:0000313|EMBL:EAK1340513.1, ECO:0000313|Proteomes:UP000330270};
RN   [1] {ECO:0000313|EMBL:EAK1340513.1, ECO:0000313|Proteomes:UP000330270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PNUSAC002537 {ECO:0000313|EMBL:EAK1340513.1,
RC   ECO:0000313|Proteomes:UP000330270};
RG   PulseNet: The National Subtyping Network for Foodborne Disease Surveillance;
RA   Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S.,
RA   Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.;
RL   Submitted (MAY-2018) 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}.
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:EAK1340513.1}.
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DR   EMBL; AACDQR010000004; EAK1340513.1; -; Genomic_DNA.
DR   Proteomes; UP000330270; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10710; -; 1.
DR   Gene3D; 3.60.15.10; -; 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   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; SSF56281; 1.
DR   TIGRFAMs; TIGR00649; MG423; 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};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01491}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          140..336
FT                   /note="Lactamase_B"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..489
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
FT   COMPBIAS        1..22
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..70
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  76813 MW;  ACF1B6B3CA5DFFD9 CRC64;
     MNENNKGNSE NTNNPNSNSK NNKRYKYRNR RKKLADSISE NSQNSTHEFS NNEKINTKKN
     STNTQPLEGE NVEKPSEKKK KRNRNLPSKL TGNEDWQIAL AECIEANRVS HENRLHPLKY
     NNSSEHKIRI TPLGGLGEIG GNISVFETNN DAIIIDIGMS FPDGTMHGVD IIIPDFDYVR
     KIKDKIRGIV ITHAHEDHIG AVPYFFKEFQ FPIYATPLAL GMISNKFEEH GLKAERKWFR
     PVEKRKVYEI GEFDIEWIHI THSIIDASTL AIKTKAGTII HTGDFKIDQT PIDGYPTDLG
     RLAHYGEEGV LCLLSDSTNS YKEGYTKSES SVGPTFDQIF ARTKGRVIMS TFSSNIHRVY
     QAITYGLKYG RKVCVIGRSM ERNLYTTMEL GYIKLDRKIF IDADEVSKYK DNEVLIVTTG
     SQGETMSALY RMATDEHKFI KIKPSDQIII SAKAIPGNEA SVSAVLDYLL KAGAKVAYQE
     FSEIHVSGHA SIEEQKLMLT LVKPKFFLPV HGEYNHINKH KETAIKCGIP EKNIYLMSDG
     DQVELCQKYI KRVKTVKTGK VFVDNQINKQ IADDVVIDRQ KLADSGIVVI IAQLDKASKT
     LINKPRVFSY GLVADKQDHA FSKEMAEVLG QFFVNVKDEV LNDPRFLENQ IRQVLRKHIF
     RKIKKYPTIV PTIFVM
//