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MNMG_CAMC5
ID   MNMG_CAMC5              Reviewed;         619 AA.
AC   A7GWM5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129};
GN   OrderedLocusNames=Ccur92_03130; ORFNames=CCV52592_1793;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC       certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT99866.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000767; EAT99866.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049751862.1; NC_009715.2.
DR   AlphaFoldDB; A7GWM5; -.
DR   SMR; A7GWM5; -.
DR   STRING; 360105.CCV52592_1793; -.
DR   EnsemblBacteria; EAT99866; EAT99866; CCV52592_1793.
DR   KEGG; ccv:CCV52592_1793; -.
DR   HOGENOM; CLU_007831_2_2_7; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000006380; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 1.10.150.570; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR044920; MnmG_C_subdom.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT   CHAIN           1..619
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345248"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         269..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   619 AA;  68815 MW;  13760815A846D02E CRC64;
     MDKFNVIVVG GGHAGIEASL AAAKMGKKTL LITILAEQIG AASCNPAIGG LAKGHLVKEI
     DALGGQMGLT TDAVGIQFRV LNESKGPAVR GSRAQIDMDR YRVYMRNLLL NTPNLEISQE
     IATEILSANE QITGVKTHLG NVYETTKLII TTGTFLNGLI HVGFNKLKAG RVGELSSINL
     SQSLRNLGLE MGRLKTGTCP RIDAKTIDFS VLERQEGDAK PAAFSFRTQH FAPEQLPCYI
     AYTNETTHEI IRSNFDKAPL FTGQIEGIGP RYCPSIEDKI NRFGDRDRHH LFIEPQTREA
     SEYYINGFST SLPYDVQVAM LRSVRGFENA RIVRHGYAIE YDYVVPTELK HSLETKKVRG
     LYLAGQINGT TGYEEAAAQG LMAGINAALN LDAKDPLVLR RDEAYIGVLI DDLVTKGTKE
     PYRMFTSRAE YRLLLREDNA ILRLGGYGRE LGLIDDETHA RIEQIRVNLA KGLEILNTRE
     FTPSKQNLEF LAGLDEDVIS EKVTLQKIVA RKSFTSEKLR KLDAFFENLD EASLEQILTE
     CKYSHYIAEQ KNQIDKMKDM MSVKIPENFS FRGISGLSNE VVEKLEKFAP PTLFAASEIS
     GITPAAIDIL HIYIKMSQR
 
 
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