YGFZ_EDWI9
ID YGFZ_EDWI9 Reviewed; 331 AA.
AC C5BAS5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN OrderedLocusNames=NT01EI_3346;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Folate-binding protein involved in regulating the level of
CC ATP-DnaA and in the modification of some tRNAs. It is probably a key
CC factor in regulatory networks that act via tRNA modification, such as
CC initiation of chromosomal replication. {ECO:0000255|HAMAP-
CC Rule:MF_01175}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01175}.
CC -!- SIMILARITY: Belongs to the tRNA-modifying YgfZ family.
CC {ECO:0000255|HAMAP-Rule:MF_01175}.
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; CP001600; ACR70484.1; -; Genomic_DNA.
DR RefSeq; WP_015872558.1; NC_012779.2.
DR AlphaFoldDB; C5BAS5; -.
DR SMR; C5BAS5; -.
DR STRING; 67780.B6E78_08415; -.
DR EnsemblBacteria; ACR70484; ACR70484; NT01EI_3346.
DR GeneID; 7959646; -.
DR KEGG; eic:NT01EI_3346; -.
DR PATRIC; fig|634503.3.peg.2973; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR OrthoDB; 1984573at2; -.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01175; tRNA_modifying_YgfZ; 1.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR023758; tRNA-modifying_YgfZ.
DR InterPro; IPR045179; YgfZ/GcvT.
DR InterPro; IPR017703; YgfZ/GcvT_CS.
DR PANTHER; PTHR22602; PTHR22602; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR03317; ygfZ_signature; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Folate-binding; Reference proteome; tRNA processing.
FT CHAIN 1..331
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_1000213745"
FT BINDING 28
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT BINDING 191
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ SEQUENCE 331 AA; 36173 MW; DE62910B1376E2FE CRC64;
MNLNAPFSPQ PPLAAEHLPL TLMRLDDWLP INVSGPDAQS YLQGQLTADL PSLAATQHTL
CGHCDAQGKL WSSLRLLRRR DGFTYLLRRS VATLQMLELK KYAVFAKASI VSDEGAVLLG
VAGAQASEAL GALFPRLPDA DAPLLQAGRS HLLYMAWPQP RYLLICDDAD EAERIFAPLS
ARARLADSAQ WLALDIESGI PLIDEPNCDS FLPQAVNLQA LGGISFTKGC YSGQEMVARA
KYRGANRRAL FWLRGSAERL PHASEDLELR LGDSWRRSGT VLAAQRLADG GVYLQAVLSS
DLPADSVLRV RDDARSQLTL SPLPYSTDQQ E