ID   YGFZ_HAMD5              Reviewed;         336 AA.
AC   C4K7V2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=HDEF_2079;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ68645.1; -; Genomic_DNA.
DR   RefSeq; WP_015874390.1; NC_012751.1.
DR   AlphaFoldDB; C4K7V2; -.
DR   SMR; C4K7V2; -.
DR   STRING; 572265.HDEF_2079; -.
DR   EnsemblBacteria; ACQ68645; ACQ68645; HDEF_2079.
DR   GeneID; 66261621; -.
DR   KEGG; hde:HDEF_2079; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   Proteomes; UP000002334; 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; IPR006222; GCV_T_N.
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   Pfam; PF01571; GCV_T; 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_1000213746"
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   336 AA;  38049 MW;  A7EADBC245FEAE24 CRC64;
     MIYQSLFSHQ ASLPSEQLPF TVILLNDWGL IRVTGKDRVK YLQGQITLDV PLLKENQHIL
     GAHCDPKGKI LSTVRLFHYL KGLAFITRKS LLHDELMELR KYAVFSKVEI DIAESTVLLG
     IAGDQARKVL KNCFEKLPTE TEPVVHEDDY SLLHFSSPRE RFLLVSQAFK EGDFLIQKLQ
     DQAVFRSSEQ WLALDIESGF PIIDAKNKTQ FIPQAANLKA LGGISFTKGC YTGQEVVART
     EYRGVNKKAL YWLTGKACRV PDVGEALEIQ MEEDYRRTGV VLAAVKLQDG SLWVQAILNH
     DFQKDSILRV KGDENGRLMI SHRSFKKFEP SSNPIA