ID   YGFZ_SODGM              Reviewed;         328 AA.
AC   Q2NRF3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=SG1997;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE75272.1; -; Genomic_DNA.
DR   RefSeq; WP_011411727.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NRF3; -.
DR   SMR; Q2NRF3; -.
DR   STRING; 343509.SG1997; -.
DR   EnsemblBacteria; BAE75272; BAE75272; SG1997.
DR   KEGG; sgl:SG1997; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   OrthoDB; 1984573at2; -.
DR   Proteomes; UP000001932; 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; tRNA processing.
FT   CHAIN           1..328
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262902"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         190
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   328 AA;  35445 MW;  8FC24A59AA1B7523 CRC64;
     MSSKVPFPPR LPLPSSHLPL TLISLEDWAL VTLNGADTVK YLQGQLTCDV ASLDADRFSF
     AAHCDAKGKM FSHLCVFHHH DGMAFIERRS VRDSQLAELK KYAVFSKTTI TADDDAVLLG
     VAGFQAQAAL GGLFTSVPNA AHPVAHHQDT TLLYFSLPAP RFLLITTPAV RDALQHKLEG
     QAQLNDSQQW LALDIEAGYP VIDSANGTQF IPQAANVQAL DGISFNKGCY AGQEMVARAK
     YRGANKRALY WLAGKASHPP AAGDDLELKM GDNWRRTGTV LAACQLEDGS VWVQAVLNND
     LASDSLLHVR DDSAGALSVQ PLPYAIGE