ID   YGFZ_COLP3              Reviewed;         324 AA.
AC   Q47WN5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=CPS_4132;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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; CP000083; AAZ25357.1; -; Genomic_DNA.
DR   RefSeq; WP_011044868.1; NC_003910.7.
DR   AlphaFoldDB; Q47WN5; -.
DR   SMR; Q47WN5; -.
DR   STRING; 167879.CPS_4132; -.
DR   EnsemblBacteria; AAZ25357; AAZ25357; CPS_4132.
DR   KEGG; cps:CPS_4132; -.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   OrthoDB; 1984573at2; -.
DR   Proteomes; UP000000547; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..324
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262887"
FT   BINDING         186
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   324 AA;  35377 MW;  575DD96BC31429D2 CRC64;
     MTITTSKQLP SLAQLPETYL IELSEFGAIS LSGEEQSKYL QGQVTCDVNS ITESNLLVGA
     HCDAKGKVFS VFRLINRSSA HLLLQPTASI EGSLKELKKF GVFAKVTIDI AEELGFIALI
     GKQASSLIQQ EFSQVPDSLT PVVQIGSTSL VYLSGEQPRY IIIDDKATIT AITEKLALPT
     YSQSVWNLLE ITQGFPILTA NTSGHYVPQM LNLQAINGIS FTKGCYLGQE TVARMQYLGK
     NKRALFCLNS QLEQPFQSDD VIEKQLGENW RKAGDILAHY QADDGSCVIQ AILANDGDLP
     ILRIASQADS VVTNQTLPYT LIAE