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Database: UniProt
Entry: B4S953_PROA2
LinkDB: B4S953_PROA2
Original site: B4S953_PROA2 
ID   B4S953_PROA2            Unreviewed;       551 AA.
AC   B4S953;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Ribonuclease, Rne/Rng family {ECO:0000313|EMBL:ACF45085.1};
GN   OrderedLocusNames=Paes_0019 {ECO:0000313|EMBL:ACF45085.1};
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF45085.1, ECO:0000313|Proteomes:UP000002725};
RN   [1] {ECO:0000313|EMBL:ACF45085.1, ECO:0000313|Proteomes:UP000002725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP001108; ACF45085.1; -; Genomic_DNA.
DR   RefSeq; WP_012504622.1; NC_011059.1.
DR   AlphaFoldDB; B4S953; -.
DR   STRING; 290512.Paes_0019; -.
DR   KEGG; paa:Paes_0019; -.
DR   eggNOG; COG1530; Bacteria.
DR   HOGENOM; CLU_003468_5_3_10; -.
DR   Proteomes; UP000002725; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd04453; S1_RNase_E; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00757; RNaseEG; 1.
DR   PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR   PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002725};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          43..105
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          95..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          358..385
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        103..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62800 MW;  7B1B8C6A325ACCA8 CRC64;
     MKKTVKKQLL MNKSGDEIQV ALVEDGRLAE LVIERPDSLR SIGDIYLGRV HKVVEGLKAA
     FVDIGQKSDG FLHFSDVGTT NEDYRALIED DEDDENGALE GEDVEKNDDV QAESKPRASE
     KAPRSATPER KRQSYTQMIA GKLKANDSIL VQVIKEPISN KGSRLTSDIT IAGRFMVLLP
     FGGGQIAVSR RVVSRKERSR LKKLVRSILP EGFGAIIRTV AENQEEELLK KDLEKLLVKW
     QQIEEKLQDA KPPQLIFKED TIISSVLRDS LNSDVTELVA NCPSIYKETL NYILWAAPEM
     EKNVTLYQGK LPLFEGYGIA KDVESIFSRK VWLKSGGYII IEHTEAMVVV DVNSGRYAAK
     KEQEENSLKT NLEAAREVVR QLRLRDIGGI IVVDFIDMLD QKNSKKVFDS MKTELRHDRA
     KSNILPLSDF GLMQITRERI RPSLMQRMGD QCPACGGSGV VQARYTTINQ IERWLRKYAL
     QRKVMFQKLD LYVSPTVAEP LCDEERKTEM KWFLQHMLFV KIKSDESLRS DDFRFYLQKN
     NKEITSEFSD L
//
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