YGFZ_SALTY
ID YGFZ_SALTY Reviewed; 326 AA.
AC Q8ZM80;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN Name=ygfZ {ECO:0000255|HAMAP-Rule:MF_01175}; OrderedLocusNames=STM3048;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL21923.1; -; Genomic_DNA.
DR RefSeq; NP_461964.1; NC_003197.2.
DR RefSeq; WP_000874172.1; NC_003197.2.
DR AlphaFoldDB; Q8ZM80; -.
DR SMR; Q8ZM80; -.
DR STRING; 99287.STM3048; -.
DR PaxDb; Q8ZM80; -.
DR EnsemblBacteria; AAL21923; AAL21923; STM3048.
DR GeneID; 1254571; -.
DR KEGG; stm:STM3048; -.
DR PATRIC; fig|99287.12.peg.3229; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR PhylomeDB; Q8ZM80; -.
DR BioCyc; SENT99287:STM3048-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
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..326
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_0000262898"
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 326 AA; 35972 MW; 65CE54FE0E1D2D29 CRC64;
MAFISFPPRH PSSSARLPLT LIALDDWALS TITGVDSEKY IQGQVTADVS QMTEQQHLLA
AHCDAKGKMW STLRLFRERD GFAWIERRSV LEAQLTELKK YAVFSKVVIA PDDERVLLGV
AGFQARAALA NVFSELPNSE NQVVRDGAST LLWFEHPAER FLLVTDVATA NMLTEKLHGE
AELNNSQQWL ALDIEAGIPV IDAANSGQFI PQATNLQALG GISFKKGCYT GQEMVARAKF
RGANKRALWL LAGKASRVPE AGEDLELQMG ENWRRTGAIL AATQLDDGQL LVQAVMNNDL
EAESVFRVRD DANTLHIVPL PYSLEE
