UVEN_MICLC
ID UVEN_MICLC Reviewed; 279 AA.
AC P46303; C5CCV3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ultraviolet N-glycosylase/AP lyase;
DE AltName: Full=Pyrimidine dimer glycosylase;
DE AltName: Full=UV-endonuclease;
DE Contains:
DE RecName: Full=UV endonuclease 32 kDa isoform;
DE Contains:
DE RecName: Full=UV endonuclease 31 kDa isoform;
GN Name=pdg; OrderedLocusNames=Mlut_18220;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-35, AND FUNCTION.
RX PubMed=7559510; DOI=10.1074/jbc.270.40.23475;
RA Piersen C.E., Prince M.A., Augustine M.L., Dodson M.L., Lloyd R.S.;
RT "Purification and cloning of Micrococcus luteus ultraviolet endonuclease,
RT an N-glycosylase/abasic lyase that proceeds via an imino enzyme-DNA
RT intermediate.";
RL J. Biol. Chem. 270:23475-23484(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity
CC and AP-lyase activity. Initiates repair at cis-syn pyrimidine dimers.
CC Proceeds via an imino enzyme:DNA intermediate.
CC {ECO:0000269|PubMed:7559510}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- MISCELLANEOUS: Readthrough of the terminator UAG occurs between codons
CC for Gly-268 and Ala-270. Two forms of 31 kDa and 32 kDa have been
CC detected.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR EMBL; U22181; AAA86508.1; ALT_TERM; Genomic_DNA.
DR EMBL; CP001628; ACS31305.1; -; Genomic_DNA.
DR STRING; 465515.Mlut_18220; -.
DR PRIDE; P46303; -.
DR EnsemblBacteria; ACS31305; ACS31305; Mlut_18220.
DR KEGG; mlu:Mlut_18220; -.
DR eggNOG; COG0177; Bacteria.
DR HOGENOM; CLU_012862_3_2_11; -.
DR Proteomes; UP000000738; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 HAMAP; MF_00942; Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR005759; Nth.
DR Pfam; PF10576; EndIII_4Fe-2S; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR TIGRFAMs; TIGR01083; nth; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; DNA damage; DNA repair; Endonuclease;
KW Glycosidase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW Reference proteome; RNA suppression of termination.
FT CHAIN 1..279
FT /note="UV endonuclease 32 kDa isoform"
FT /evidence="ECO:0000305"
FT /id="PRO_0000001742"
FT CHAIN 1..268
FT /note="UV endonuclease 31 kDa isoform"
FT /id="PRO_0000001743"
FT DOMAIN 123..142
FT /note="HhH"
FT REGION 255..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT CONFLICT 172..185
FT /note="GKGRARRGRPVPPA -> VKVEHAVGALFPR (in Ref. 2;
FT ACS31305)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="R -> A (in Ref. 2; ACS31305)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="A -> G (in Ref. 2; ACS31305)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..279
FT /note="AGAAGPRPRAGGXAPGLPAQPFR -> RRELRALGHGLEA (in Ref. 2;
FT ACS31305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30471 MW; C385369A1827C005 CRC64;
METESTGTPT GETRLALVRR ARRIDRILAE TYPYAVAELD FETPFELLVA TVLSAQTTDV
RVNAATPALF ARFPDAHAMA AATEPELQEL VRSTGFYRNK ASAILRLSQE LVGRHDGEVP
ARLEDLVALP GVGRKTAFVV LGNAFGQPGI TVDTHFGRLA RRLGFTDETD PGKGRARRGR
PVPPARDWTM LSHRLIFHGR RVCHARRPAC GRCPIARWCP SYAAGETDPE RARALLAYEL
KPGREELLEL LRAGRTAGAA GPRPRAGGXA PGLPAQPFR
