Y1434_METJA
ID Y1434_METJA Reviewed; 220 AA.
AC Q58829;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative DNA repair glycosylase MJ1434 {ECO:0000305};
GN OrderedLocusNames=MJ1434;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PRELIMINARY FUNCTION AS AN URACIL-DNA GLYCOSYLASE.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=12682355; DOI=10.1093/nar/gkg319;
RA Chung J.H., Im E.K., Park H.Y., Kwon J.H., Lee S., Oh J., Hwang K.C.,
RA Lee J.H., Jang Y.;
RT "A novel uracil-DNA glycosylase family related to the helix-hairpin-helix
RT DNA glycosylase superfamily.";
RL Nucleic Acids Res. 31:2045-2055(2003).
RN [3]
RP SHOWS THAT IT HAS NO URACIL-DNA GLYCOSYLASE ACTIVITY, AND MUTAGENESIS OF
RP GLU-132.
RX PubMed=20410075; DOI=10.1093/nar/gkq270;
RA Schomacher L., Smolorz S., Ciirdaeva E., Ber S., Kramer W., Fritz H.J.;
RT "Helix-hairpin-helix protein MJ1434 from Methanocaldococcus jannaschii and
RT EndoIV homologue TTC0482 from Thermus thermophilus HB27 do not process DNA
RT uracil residues.";
RL Nucleic Acids Res. 38:5119-5129(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AB83};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P0AB83};
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have uracil-DNA glycosylase
CC activity, but further protein analysis show that it does not exhibit
CC DNA uracil glycosylase activity when produced in an Ung-deficient
CC Escherichia coli host. {ECO:0000269|PubMed:12682355,
CC ECO:0000269|PubMed:20410075}.
CC -!- CAUTION: Lacks the lysine residue within the HhH motif critical for AP
CC lyase activity. {ECO:0000305}.
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DR EMBL; L77117; AAB99444.1; -; Genomic_DNA.
DR PIR; A64479; A64479.
DR AlphaFoldDB; Q58829; -.
DR SMR; Q58829; -.
DR STRING; 243232.MJ_1434; -.
DR EnsemblBacteria; AAB99444; AAB99444; MJ_1434.
DR KEGG; mja:MJ_1434; -.
DR eggNOG; arCOG00461; Archaea.
DR HOGENOM; CLU_012862_6_0_2; -.
DR InParanoid; Q58829; -.
DR OMA; GPQGWWP; -.
DR PhylomeDB; Q58829; -.
DR BRENDA; 3.2.2.27; 3260.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..220
FT /note="Putative DNA repair glycosylase MJ1434"
FT /id="PRO_0000102244"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AB83"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AB83"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AB83"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P0AB83"
FT MUTAGEN 132
FT /note="E->K: Shows AP lyase activity."
FT /evidence="ECO:0000269|PubMed:20410075"
SQ SEQUENCE 220 AA; 25938 MW; BB3188BE152995F6 CRC64;
MKENKFEMIY KIYKILLDYY GHQNWWPAET RYEVVVGAIL TQNTSWKNVE RAINNLKMED
LLEEVKILNV DEDKLKELIR PAGFYNLKAK RLKNVTKFIV ENYGNTEEMA KTDKDTLILR
AELLSINGVG KETADSILLY ALDRESFVVD AYTKRMFSRL GVINEKAKYD EIKEIFEKNL
PKDLEIYKEY HALIVEHCKK FCRKKALCDN CPIKEFCLSK
