ID A0A221W086_9PSEU Unreviewed; 949 AA.
AC A0A221W086;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ribonuclease G {ECO:0000313|EMBL:ASO19179.1};
DE EC=3.1.26.- {ECO:0000313|EMBL:ASO19179.1};
GN Name=rng {ECO:0000313|EMBL:ASO19179.1};
GN ORFNames=AHOG_07670 {ECO:0000313|EMBL:ASO19179.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO19179.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO19179.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO19179.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022521; ASO19179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221W086; -.
DR KEGG; ahg:AHOG_07670; -.
DR Proteomes; UP000204221; 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; 1.10.10.2480; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR006847; IF2_N.
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; PF04760; IF2_N; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ASO19179.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000204221};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 369..446
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 101922 MW; 7A74ACE9A52CF302 CRC64;
MKNVPADERS GTAEAPAGGA ELELPAKLRV HALAKLLEVR SKDVLTALET LGAEVRSAQS
SVSRELALQV IEKLAPAQEA TRTQRVDAAE EPAAEPAGED VGPRAAAAPV FAPPQPVFLP
PQPAAAPAAR PAPAKQSPAP ATQTQQPEPV VEPQTTSPAA TEDVDEDEDA GGRRRRRRGR
RGRGRGRGGQ DAEGVDEHGE DEEITSAEAA TDTAPETPAE EPETAESDTE DSDGEQAEGS
RRRRRRRRRK GTGEDDTASR SDDPPNTVVH VRESKPAQAK ADTVVEDEVR SVRGSTRLEA
KRQRRRDGRE AGRRRVPVLS EAEFLARRES VERRMIVRER GDRTQIAVLE DGVLVEHFVT
SSGTGSIVGN VYLGRVQNVL PSMEAAFVDI GRGRNAVLYA GEVDWDAAGL EGKARKIEQA
LSTGDSVLVQ VTKEPVGHKG ARLTTQISLP GRFLVYVPGG GATGISRKLP DVERKRLKEI
LKRIVPDEAG VIIRTASEGT SEEALDRDVR RLRAQWEVIK ERAAVPRAQA PQLLYEEPDL
LIKVVRDLFT EDFSGLVVQG DGAWDTIESY VNHVAPDLVS RLRRHVGLKD VFTEHRVDEQ
LAKALDRKVW LPSGGYLVID RTEAMTVVDV NTGKFTGSGG NLEETVTRNN LESVEEIVRQ
LRLRDIGGII VIDFIDMVLE SNRDLVLRRL TECLGRDRTR HQVAEVTSLG LVQMTRKRVG
TGLLEAYSTT CEHCRGRGVI VSTEPVGAGG ASTSGGNSHT SGNGTTSHQH QHGAAAGAQI
NGAGSTDKQN GSASASSRRS RPRGKGNVVV DTVAETPAQA TEHAVETQTE NSRENGDAPR
QGRRQTKAEA RAEAKAKAAR EAEAARATES ARPAEPANEL PPAQEQQAAE PGRRNGHPVE
TPADLEPAAE PAASAAAAVT PAAAPARRQR RRAAARPAGP PKGNQAGEE
//
