ID G7H568_9ACTN Unreviewed; 981 AA.
AC G7H568;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative ribonuclease {ECO:0000313|EMBL:GAB10993.1};
GN ORFNames=GOARA_063_01920 {ECO:0000313|EMBL:GAB10993.1};
OS Gordonia araii NBRC 100433.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB10993.1, ECO:0000313|Proteomes:UP000035088};
RN [1] {ECO:0000313|EMBL:GAB10993.1, ECO:0000313|Proteomes:UP000035088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB10993.1,
RC ECO:0000313|Proteomes:UP000035088};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia araii NBRC 100433.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:GAB10993.1}.
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; BAEE01000063; GAB10993.1; -; Genomic_DNA.
DR RefSeq; WP_007323068.1; NZ_BAEE01000063.1.
DR AlphaFoldDB; G7H568; -.
DR STRING; 1073574.GOARA_063_01920; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000035088; Unassembled WGS sequence.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 378..455
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 105583 MW; D10FF487CA34E425 CRC64;
MTENGSPTDA NASGPAAELP DKMRVHALAR LMGATSRDVL EHLEALGSAV RSASATIDRD
VAERVIDRAG GLPSAETPET AEAAPAPPVA ETLFSAAAEV SDAPITTAAP EAVNPLFLPP
QAPEPAPRAD DDADIEQADA DRDASETESS DDESDDQAGR SRRRRRGRRG RGRGRGEGNG
EDTNADDTNG DADDNATVDA DKTAESSTTD TATSDSEKPE GEQSENGDGE ESDGEGSGAT
ATSKRRRRRR RRKGGADGGE EASPDDPPNT VVHEREPRSK RARDEVQGIS GSTRLEAKRQ
RRRDGRDAGR RRPPILSESE FLARREAVER VMVVREKVHT SAERDAGAHE DYTQVAVLED
GVLVEHFVTT ANSTSLVGNI YLGRVQNVLP GMEAAFVDIG RGRNGVLYAG EVNWEAAGLD
GGSRKIEQAL KPGDNVLVQV SKDPVGHKGA RLTTQVSLAG RYLVYVPGGS STGISRKLPD
VERKRLKSIL AKIVPDGAGV IIRTASEGIS ADDLEADIKR LEAQWRKIDA DAQGATGKSG
KSVSPKALYE EPDLLVRVVR DLFNEDFRKL VVEGQTAWSL VERYITDVAP DLMDRVEKFE
KPGPDAPDSF VVHRIDEQLA KALDRKVWLP SGGTLIIEHT EAMTVVDVNT GKFTGSGGNL
EETVTRNNLE AAEEIVRQMR LRDLGGMIVV DFIDMVLESN RDLVLRRLTE ALARDRTRHQ
VSEVTSLGLV QMTRKRLGTG LLEAFSTTCT HCAGRGVIVH ADPVEVRGSE DSGREGGSSK
RSRRKGRKSE PVAESKAPAH NPAEHPLFRA MHAHIHENDE IETVDADEAD LDIAATGTSE
STAPPEFDDE TASESVATPV SEPIATTAEP ELEVAPVEPE LEVAPVEPEP EVAEPASESE
REPVDQPVRK PRHRRVRRAP VSTGSGTTIV IGSDEHDETP AVSRTTAGPI AEQSDVEAVA
VVRRPRRRAA SRPSGAPQHE A
//