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Database: UniProt
Entry: A0A1I5EYI8_PARPN
LinkDB: A0A1I5EYI8_PARPN
Original site: A0A1I5EYI8_PARPN 
ID   A0A1I5EYI8_PARPN        Unreviewed;       558 AA.
AC   A0A1I5EYI8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Ribonuclease J {ECO:0000313|EMBL:RKS52495.1};
GN   ORFNames=BDE18_1822 {ECO:0000313|EMBL:RKS52495.1}, HYQ43_10120
GN   {ECO:0000313|EMBL:QLH14658.1};
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=82367 {ECO:0000313|EMBL:RKS52495.1, ECO:0000313|Proteomes:UP000273626};
RN   [1] {ECO:0000313|EMBL:RKS52495.1, ECO:0000313|Proteomes:UP000273626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 /
RC   NCCB 82005 / GB17 {ECO:0000313|Proteomes:UP000273626}, and DSM 2944
RC   {ECO:0000313|EMBL:RKS52495.1};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QLH14658.1, ECO:0000313|Proteomes:UP000509322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC10489 {ECO:0000313|EMBL:QLH14658.1,
RC   ECO:0000313|Proteomes:UP000509322};
RA   Si Y.;
RT   "The complete genome of Paracoccus pantotrophus ACCC 10489.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP058690; QLH14658.1; -; Genomic_DNA.
DR   EMBL; RBLI01000001; RKS52495.1; -; Genomic_DNA.
DR   RefSeq; WP_024843151.1; NZ_RIAQ01000012.1.
DR   AlphaFoldDB; A0A1I5EYI8; -.
DR   GeneID; 51371484; -.
DR   OrthoDB; 9770211at2; -.
DR   Proteomes; UP000273626; Unassembled WGS sequence.
DR   Proteomes; UP000509322; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   InterPro; IPR042173; RNase_J_2.
DR   InterPro; IPR041636; RNase_J_C.
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   4: Predicted;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          17..207
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   558 AA;  60760 MW;  8B228A960C253628 CRC64;
     MAERLIYLPL GGAGEIGMNA YVYGYGQPGR ERLIVVDLGV TFGDMDSAPG IDLIMADVAW
     LEANRDRIDA IFITHGHEDH VGALGLLWPR LQKPVHCRRF TGALARLKLE EAGQPVDQLH
     IHAPRPDVVT AGPFRVQFVP VSHSIPESSA LIIDTPAGRI VHTGDFKLDG TPVVGEAFDP
     ILWHDIANEG QGIKVLTCDS TNVFSPHPGR SEAVLATPLL DFVMAQRQMV VATTFASNIA
     RLKTLAEAGI AAGRKICLLG RAMRRMVTVG IETGILTNFP SFISPEEASE LPRDKVMLIV
     TGSQGERRAA SAQLSRGRYL GIELKEGDSF LFSSRTIPGN ERGVIRIMNA LSEMGVDLYD
     ADDGLYHVSG HANRPDIEAV HDLLKPQIVI PMHGEHMHLR EHAKLAEARG IHSVVATNGT
     MLDLSGEAPR VVDQIDTGRI YLDGTVLIGA MDGVVRDRIR MALNGHAMVS VIIDEDDTPL
     PDAWVELSGL PEKGRAGVPL ARNIEAELAG FLERADDRTV MDDDRLEEAI RKITRQVSME
     EIGKKPEVTV VISRLAAE
//
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