ID A5WCI8_PSYWF Unreviewed; 613 AA.
AC A5WCI8;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=RNAse G {ECO:0000313|EMBL:ABQ93379.1};
DE EC=3.1.4.- {ECO:0000313|EMBL:ABQ93379.1};
GN OrderedLocusNames=PsycPRwf_0424 {ECO:0000313|EMBL:ABQ93379.1};
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93379.1};
RN [1] {ECO:0000313|EMBL:ABQ93379.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93379.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) 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; CP000713; ABQ93379.1; -; Genomic_DNA.
DR AlphaFoldDB; A5WCI8; -.
DR STRING; 349106.PsycPRwf_0424; -.
DR KEGG; prw:PsycPRwf_0424; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_6; -.
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; IPR048583; RNase_E_G_thioredoxin-like.
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; PF20833; RNase_E_G_Thio; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABQ93379.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 527..610
FT /note="RNase E/G thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF20833"
SQ SEQUENCE 613 AA; 68925 MW; BE8A34DED610FDD0 CRC64;
MSEELLINVS PMESRVAVLD NGVVSEVYIE RHNKLGLVGN IYLGTVVRVL PGMQAAFVEI
GQSRTAFLHV NDMRRIARPA PTADKAPEIR HNAKQEPTVL TSMPVDRCEH IAENVVTASD
TMASVIAETE PAMEADPLSA KTEIEAGSLR EKKSALADES DNLKNDLLDN ALLEIDSPDM
VGNAITKADT KPAAVKERQI IEPPRHELIQ YRLHEGQKIL VQVTKDQLGT KGARLTTNIS
LPSRYLVYLP SSEHIGISQR IDNEEERHRL KTELGALMQT VNLTGGLIAR TAAERVPVAK
LEEDIYYLVQ LWRTIQARKE ASAGSGQSAV LIYQELSLPL RSIRDLVHPD TEKVIVDHEG
MYNEVRQFAK EFVPFIYPRI LPYSGEQPLF DVHRVEEDLR DALKRRVDLK SGGYLIIDQT
EAMTTIDVNT GSFVGGRSLE DTVYKTNLEA THAIARQLRL RNLGGIIILD FIDMLEQQHK
DDVLENLQYQ LSQDYAKTKI TQVSELGLVE MTRKRTRESL EQQLCEPCKT CEGKGFIKTA
ETVCFEIFRE IMRCARTYNS PKKFTVVAHA SVIDLLLSSE ADTVADLEYL LGRVITFEVE
NLYTQEQYDI VLD
//