YGFZ_VIBC3
ID YGFZ_VIBC3 Reviewed; 323 AA.
AC A5F5F3; C3M4W3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN OrderedLocusNames=VC0395_A2049, VC395_2587;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ21867.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10574.1; -; Genomic_DNA.
DR RefSeq; WP_000384072.1; NZ_JAACZH010000010.1.
DR AlphaFoldDB; A5F5F3; -.
DR SMR; A5F5F3; -.
DR STRING; 345073.VC395_2587; -.
DR EnsemblBacteria; ABQ21867; ABQ21867; VC0395_A2049.
DR KEGG; vco:VC0395_A2049; -.
DR KEGG; vcr:VC395_2587; -.
DR PATRIC; fig|345073.21.peg.2491; -.
DR eggNOG; COG0354; Bacteria.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR Proteomes; UP000000249; Chromosome 2.
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; tRNA processing.
FT CHAIN 1..323
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_1000073080"
FT BINDING 29
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT BINDING 182
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ SEQUENCE 323 AA; 36109 MW; 215BCD86A31A1985 CRC64;
MDWQNRFSVL NLSSHDPLPE LMLTHLTGWG AITLVGTDKK AYLQGQVTCN VVSLQEQQVT
FGAHCDAKGK VWSVFRLFHH HDGYAMFQPQ SAMEVELREL KKYAIFSKVT IAESSDIALG
VMGSQADAWI DTVSETTGDV RRIAGGTAVR MSPQRWLLLV NAEQAEQYVN AWQGLHVEQS
LWTRMDIEEA VPVVTQTAQN EHIPQALNVQ AVDGISFTKG CYTGQETVAR AKYRGINKRA
MYIVKGNLSA PLSQDEPVVL ERAVGENWRS AGALLTYYRF TDSIAIGLIV LPNDLEHDVE
LRLAAQPDTR WHIQPLPYSL SEE
