ID   YGFZ_BLOFL              Reviewed;         336 AA.
AC   Q7VRF7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=Bfl260;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83331.1; -; Genomic_DNA.
DR   RefSeq; WP_011126540.1; NC_005061.1.
DR   AlphaFoldDB; Q7VRF7; -.
DR   SMR; Q7VRF7; -.
DR   STRING; 203907.Bfl260; -.
DR   EnsemblBacteria; CAD83331; CAD83331; Bfl260.
DR   KEGG; bfl:Bfl260; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   OrthoDB; 1984573at2; -.
DR   Proteomes; UP000002192; 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..336
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262885"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         193
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   336 AA;  39274 MW;  D37496C1E6A77789 CRC64;
     MLSKTNFIKQ PIVHSSVLPL TLMFLKNWIL IKLQGTDIIQ YLHNQFTCDI KNLNKNQYSF
     AAHCNFNGRM ISNMYVFYIN NQKIAFIEPL NIHHKQISIM QKYATFSNVT ITPDYNVTLI
     GASGLYVKKY LNTFFTTLPD TKNMVIHYPG ITLLHFKLPI DRFLLIIYDQ TILDFLLNKT
     QSFPIYYNSY HQWTALDIEA GYPYIDFATS ELFFPQAANM DILQGISFNK GCYIGQELVA
     RIQHYKLNKQ SLYQLTSNTY HNQHNQLPVS GDHIVLRQKN NQIWKHIGTV LQSCQMQEGN
     ICIQAILNKS FIKETEVYFQ HNELIYSNIN LKILEK