ID   YGFZ_BUCAI              Reviewed;         319 AA.
AC   P57510;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, 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=BU435;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13133.1; -; Genomic_DNA.
DR   RefSeq; NP_240247.1; NC_002528.1.
DR   RefSeq; WP_009874388.1; NC_002528.1.
DR   AlphaFoldDB; P57510; -.
DR   SMR; P57510; -.
DR   STRING; 107806.10039099; -.
DR   EnsemblBacteria; BAB13133; BAB13133; BAB13133.
DR   KEGG; buc:BU435; -.
DR   PATRIC; fig|107806.10.peg.444; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   BioCyc; BAPH107806:GBZJ-428-MON; -.
DR   Proteomes; UP000001806; 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..319
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000216253"
FT   BINDING         27
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         189
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   319 AA;  37100 MW;  021D7B17DEB52A9E CRC64;
     MPSFISIQNI IYPSNELSLT MILLEEWSLT YVEGIDSKKY LQGQLTIDIN LLLKTHHTLC
     AHCNFNGRVW STMHLFHYEK GYAYIQRKSV SQIQIKEICK YSIFSKIKIR ELNSICLIGF
     AGCNVRSFLS SLFVKIPNQS CPVIHEDNKT ILWYEKPSER FLLVLPFLDF LTLKRKINQN
     IFLNNSKQWL LLDIEAGLPV IDKICSNKFT PQAINLHNLK AISFKKGCYY GQETIARIFF
     KKTNKYFLCF LVSTGSIFPK IGSFIETKVD SEWFKVGVLL SIVHVKCEEI YIQVVLRKSV
     NINNLFRIHG FENIFLIKN