ID   A0A366I5X9_9GAMM        Unreviewed;       328 AA.
AC   A0A366I5X9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000256|HAMAP-Rule:MF_01175};
GN   ORFNames=DES54_11015 {ECO:0000313|EMBL:RBP63717.1};
OS   Brenneria salicis ATCC 15712 = DSM 30166.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=714314 {ECO:0000313|EMBL:RBP63717.1, ECO:0000313|Proteomes:UP000253046};
RN   [1] {ECO:0000313|EMBL:RBP63717.1, ECO:0000313|Proteomes:UP000253046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 30166 {ECO:0000313|EMBL:RBP63717.1,
RC   ECO:0000313|Proteomes:UP000253046};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_01175}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01175}.
CC   -!- SIMILARITY: Belongs to the tRNA-modifying YgfZ family.
CC       {ECO:0000256|HAMAP-Rule:MF_01175}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RBP63717.1}.
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DR   EMBL; QNRY01000010; RBP63717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366I5X9; -.
DR   OrthoDB; 9796287at2; -.
DR   Proteomes; UP000253046; Unassembled WGS sequence.
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   Gene3D; 2.40.30.160; -; 1.
DR   Gene3D; 3.30.70.1630; -; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
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   InterPro; IPR048451; YgfZ_barrel.
DR   NCBIfam; TIGR03317; ygfZ_signature; 1.
DR   PANTHER; PTHR22602:SF0; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22602; UNCHARACTERIZED; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF21130; YgfZ_barrel; 1.
DR   PIRSF; PIRSF006487; GcvT; 2.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01175};
KW   Folate-binding {ECO:0000256|ARBA:ARBA00022954, ECO:0000256|HAMAP-
KW   Rule:MF_01175};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01175}.
FT   DOMAIN          32..143
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          245..312
FT                   /note="tRNA-modifying protein YgfZ-like beta-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF21130"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01175"
FT   BINDING         190
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   328 AA;  35732 MW;  3BA20B5EE1D9027B CRC64;
     MANPFPFASQ RPCASARLPA TLISLDDWAL ATLTGPDTIK YLQGQVTADV AALPADQHIL
     CAHCDAKGKM WSSLRLFQRG DGFAFIERRN LRDAQLSELK KYAVFSKTTI AAEDNVVLLG
     AAGARVRELL SSVFSTLPDA GHPVVQVEDA TLLHFSLPAE RFLLVLTPAR STSLIAQLEG
     KTALNDSRQW LALDIEAGLP IIDSANSTQF IPQATNLQAL NGISFSKGCY AGQEMVARAK
     YRGANKRALY WLAGQASRVP KAGEDLELQL GENWRRTGTV LAACRLQDES VWIQVVMNND
     LAGDSLLRVR GDADGQLKIQ PLPYEITD
//