YGFZ_SHIF8
ID YGFZ_SHIF8 Reviewed; 326 AA.
AC Q0T0Z9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN Name=ygfZ {ECO:0000255|HAMAP-Rule:MF_01175}; OrderedLocusNames=SFV_2946;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000266; ABF05016.1; -; Genomic_DNA.
DR RefSeq; WP_000886062.1; NC_008258.1.
DR AlphaFoldDB; Q0T0Z9; -.
DR SMR; Q0T0Z9; -.
DR EnsemblBacteria; ABF05016; ABF05016; SFV_2946.
DR GeneID; 66673228; -.
DR KEGG; sfv:SFV_2946; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR BioCyc; SFLE373384:SFV_RS16345-MON; -.
DR Proteomes; UP000000659; 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..326
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_1000065778"
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; 36094 MW; 08E050CE26B56B77 CRC64;
MAFTPFPPRQ PTASARLPLT LMTLDDWALA TITGADSEKY MQGQVTADVS QMAEDQHLLA
AHCDAKGKMW SNLRLFRDGD GFAWIERRSV REPQLTELKK YAVFSKVTIA PDDERVLLGV
AGFQARAALA NLFSELPSKE KQVVKEGATT LLWFEHPAER FLIVTDEATA NMLTDKLRGE
AELNNSQQWL ALNIEAGFPV IDAANSGQFI PQATNLQALG GISFKKGCYT GQEMVARAKF
RGANKRALWL LAGSASRLPE AGEDLELKMG ENWRRTGTVL AAVKLEDGQV VVQVVMNNDM
EPDSIFRVRD DANTLHIEPL PYSLEE