ID S3NWC4_9GAMM Unreviewed; 484 AA.
AC S3NWC4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Ribonuclease G {ECO:0000313|EMBL:EPF70946.1};
GN ORFNames=F945_02709 {ECO:0000313|EMBL:EPF70946.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF70946.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF70946.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF70946.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) 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:EPF70946.1}.
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DR EMBL; ATGI01000034; EPF70946.1; -; Genomic_DNA.
DR RefSeq; WP_016657094.1; NZ_KE340354.1.
DR AlphaFoldDB; S3NWC4; -.
DR STRING; 632955.GCA_000829675_01307; -.
DR PATRIC; fig|421052.3.peg.2645; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_6; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000014568; 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; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
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:UP000014568};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..113
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 484 AA; 55207 MW; 0FC8C7BBDDE5CDFD CRC64;
MSDELLINVT PMECRVALVE NGTVNELFVE RSVKRGLVGN IYKAKVVRVL PGMQAAFVDI
GLSRTAFLHI NDMVWPRNQP TPNVYELLQP GQILTVQVMK DMLGTKGARL STDLSIPSRY
LVLMPFGNYI GVSQRIESET ERERLRGIIE NIQKEHQLPG SVIVRTAAEG VDEAAIARDM
CYLAKLWEYI QKKQRSIVVP SLIFEELPLP QRVIRDLVSE KTAKIYVDSR EIHAKLQDFV
REFVPTAENR LFHYPGERPI FDLYNVEEDV QKALQTRVAL KSGGYLMIDQ TEAMTTIDVN
TGSYVGGRSL EDTVFKTNME ATQVIARQLR LRNLGGIIII DFIDMQEASH RDDVLMQFEK
MLERDHAKTK ITQVSELGLV EMTRKRTRES LEHLLCESCP TCQGRGYVKT AETVCYEIFR
EILRYARAFE SQSGFTVIAH PQVIDRLLTG EAAAVADLEH FIDRVIKFQV ENLYTQEQYD
VILS
//
