ID B0PFA2_9FIRM Unreviewed; 832 AA.
AC B0PFA2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=ANACOL_03481 {ECO:0000313|EMBL:EDS10035.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS10035.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS10035.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10035.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS10035.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10035.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS10035.1}.
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DR EMBL; ABGD02000025; EDS10035.1; -; Genomic_DNA.
DR AlphaFoldDB; B0PFA2; -.
DR STRING; 169435.ERS852551_00409; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_2_9; -.
DR Proteomes; UP000003803; 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 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.
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 296..491
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 149..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 641..645
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491"
SQ SEQUENCE 832 AA; 91451 MW; 6A956450D8EA840B CRC64;
MGDTAFALGL FVMGNSRSLF ALMACLETEK IQKMVFSDFD SLLCAPTVRI FKLEPVYTAG
GCRTGEEFCA RSRRIFAGVR RPAKNLTPSV GRRPAWTALG DCEYRFSDCD CSNTEVYFVT
DDKKVGGKLT EEQLSMGVEA LEKRSVVERA APRKKKTRQP VKETAARLLQ KVTPEQAEET
SAKPAAKKSA SRAEKPAKKE PQKRDAAKKE PARKEPAKKE PSVKKENGEP RQPKRGRKPS
PKASAPIGAT IELSEAGKAR QEKAARPAGR AKKSRVKEQR KTPVRIIPLG GLLEVGKNIT
VYECMNDMFI VDCGMTFPDE NMLGVDLVLP DFTYVQKNRD KLRGIVITHG HEDHIGALPY
FLKQINVPVY ATRLTLGLIE NKLREHGLYG KVKLVQIAPR ETIKLGCMEV EFIRVNHSIP
DAVALAIHTP AGVIIQTGDF KIDYTPIIGD IIDLARFGEL GGQGVLALLS DSTNAERPGF
TPTEVTVADS FDKLFKQAGH KRIIIATFSS NIHRMQLICE AAAKHGRKVA VSGRSMINAV
AVSTELGYLK PPNGVMIDID DINRYRPEDI VLITTGSQGE PMSALSRMAS NDHRKVTVTP
DDFIIISATP IPGNEKTVGR VVNELMRLGA DVIYERMYEV HVSGHACQEE LKIMLALTKP
KFFFPVHGEY KQLKRHASLG LAMGIPTENI FIGENGHVFE LDGVSVKTGE IVPSGRVLVD
GLGVGDVGSI VLRDRKHLGE DGLIVVVTTI DGTSGEIVAG PDIISRGFVY VREAEDMLSE
ARAIAKQTVQ DCVGGRMRDW GNIKTQVRDA LSSYFYGRTK RSPMILPVIQ EV
//
