ID W5W169_9PSEU Unreviewed; 509 AA.
AC W5W169;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN ORFNames=KALB_902 {ECO:0000313|EMBL:AHH94276.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH94276.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH94276.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH94276.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000086};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP007155; AHH94276.1; -; Genomic_DNA.
DR RefSeq; WP_025354530.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W169; -.
DR STRING; 1449976.KALB_902; -.
DR KEGG; kal:KALB_902; -.
DR PATRIC; fig|1449976.3.peg.905; -.
DR eggNOG; COG0122; Bacteria.
DR eggNOG; COG2169; Bacteria.
DR HOGENOM; CLU_000445_72_6_11; -.
DR OrthoDB; 9811249at2; -.
DR Proteomes; UP000019225; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 3.40.10.10; DNA Methylphosphotriester Repair Domain; 1.
DR Gene3D; 3.30.310.20; DNA-3-methyladenine glycosylase AlkA, N-terminal domain; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR035451; Ada-like_dom_sf.
DR InterPro; IPR004026; Ada_DNA_repair_Zn-bd.
DR InterPro; IPR010316; AlkA_N.
DR InterPro; IPR037046; AlkA_N_sf.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR PANTHER; PTHR43003; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR PANTHER; PTHR43003:SF13; DNA-3-METHYLADENINE GLYCOSYLASE 2; 1.
DR Pfam; PF02805; Ada_Zn_binding; 1.
DR Pfam; PF06029; AlkA_N; 1.
DR Pfam; PF12833; HTH_18; 1.
DR SMART; SM01009; AlkA_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF57884; Ada DNA repair protein, N-terminal domain (N-Ada 10); 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 104..202
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
SQ SEQUENCE 509 AA; 54171 MW; 5597DBA54273E983 CRC64;
MADFRQPEPV GAGSIRYVPI DSEAAYRAVA SRDARFDGHF ITAVRTTGIY CRPSCPAVRP
KRENVDFYPT AAAAQSAGFR ACRRCLPDAV PGSPEWNLRA DLAARSMRLI SDGVVERDGI
PGLARRLGYS ERHLARVLTA ELGAAPLALA RAHRAHSARL LIESTDLPFS DIAFASGFAS
IRQFNDTVRA VFATTPSQLR TAAARHKRPA PTPGRITLRL PFRPPMDSAG LLTFLAARAV
PGVEEVTEGG YARTLRLAHG PATARLTPNP EHVECSLWLA DLRDLGSAVS RLRRLLDLDA
DPAACDELLA GDPALAASVA ATPGIRLPGA VDGSEVVLRA LLGQQVSVAA ARTALTRLVT
ELGEPLQTPD GSLTRLFPTP EAIAAHAGEL LTGPRRRTDT VLSVSAALAN GSLTVDVGRD
PEELRAELEA LPGVGPWTAG YVVMRVLGMT DVLLTGDLAL RKGAAALGLP SDVDGLTERA
AAWRPWRSYA GMHLWRAAAI APPLTRRTT
//
