ID D8A533_ECOMS Unreviewed; 282 AA.
AC D8A533;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN Name=alkA {ECO:0000313|EMBL:EFK21700.1};
GN ORFNames=HMPREF9530_01626 {ECO:0000313|EMBL:EFK21700.1};
OS Escherichia coli (strain MS 21-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK21700.1, ECO:0000313|Proteomes:UP000005688};
RN [1] {ECO:0000313|EMBL:EFK21700.1, ECO:0000313|Proteomes:UP000005688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK21700.1,
RC ECO:0000313|Proteomes:UP000005688};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC {ECO:0000256|ARBA:ARBA00010817}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFK21700.1}.
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DR EMBL; ADTR01000152; EFK21700.1; -; Genomic_DNA.
DR RefSeq; WP_000288418.1; NZ_GG772672.1.
DR AlphaFoldDB; D8A533; -.
DR HOGENOM; CLU_000445_72_3_6; -.
DR Proteomes; UP000005688; Unassembled WGS sequence.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd00056; ENDO3c; 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 InterPro; IPR010316; AlkA_N.
DR InterPro; IPR037046; AlkA_N_sf.
DR InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR PANTHER; PTHR43003; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR PANTHER; PTHR43003:SF13; DNA-3-METHYLADENINE GLYCOSYLASE 2; 1.
DR Pfam; PF06029; AlkA_N; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM01009; AlkA_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55945; TATA-box binding protein-like; 1.
DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycosidase {ECO:0000313|EMBL:EFK21700.1};
KW Hydrolase {ECO:0000313|EMBL:EFK21700.1}.
FT DOMAIN 1..112
FT /note="DNA-3-methyladenine glycosylase AlkA N-terminal"
FT /evidence="ECO:0000259|SMART:SM01009"
FT DOMAIN 130..276
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 282 AA; 31295 MW; 49F58B3402E54CB2 CRC64;
MYTLNWQPPY DWSWMLGFLA ARAVSSVETV ADSYYARSLA VGEYRGVVTA IPDIARHTLH
INLSAGLEPV AAECLAKMSC LFDLQCNPQI VNGALGKLGA ARPGLRLPGS VDAFEQGVRA
ILGQLVSVAM AAKLTARVAQ LYGERLDDFP DYVCFPTPQR LAAADPQALK ALGMPLKRAE
ALIHLANAAL EGTLPMTIPG DVEQAMKKLQ TFPGIGRWTA NYFALRGWQA KDVFLPDDYL
IKQRFPGMTP AQIRRYAERW KPWRSYALLH IWYTEGWQPD EA
//