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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}.
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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
 
 
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