ID   YGFZ_BLOPB              Reviewed;         330 AA.
AC   Q493E3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=BPEN_268;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40899.1; -; Genomic_DNA.
DR   RefSeq; WP_011282806.1; NC_007292.1.
DR   AlphaFoldDB; Q493E3; -.
DR   SMR; Q493E3; -.
DR   STRING; 291272.BPEN_268; -.
DR   PRIDE; Q493E3; -.
DR   EnsemblBacteria; AAZ40899; AAZ40899; BPEN_268.
DR   KEGG; bpn:BPEN_268; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   BioCyc; CBLO291272:BPEN_RS01315-MON; -.
DR   Proteomes; UP000007794; 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; tRNA processing.
FT   CHAIN           1..330
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262886"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         192
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   330 AA;  38263 MW;  81B341647B9588B9 CRC64;
     MFPRVAFLGQ YPVPSKDLPL TFISLEEWTL VRLHGPDVIQ CLHNQFTCDI QNLNKHKYSF
     AAHCNPKGKM ISNLYVFHLK NQEMAFIERL NICKKQIEEM KKYMVFSNVT VIPDYNAILI
     GIAGTNARNH LSMFFSVLPN KTHTIIHTQD VTLLYLSSPS ERFLLIINKK SVLDYLLNES
     QSQIQFNDSR QWVSLDMEAG YPIIEPITSE LFIPQAVNMD ILDGISFNKG CYIGQESIAR
     IKYRGYNKQT LYRLNGVMDY KKNYNLPAAG DQVELKINNQ HWKNVGIVLQ SCQIKKDNIW
     VQVVLNRSIL EPSELRITNT QTHDNLMFYY