ID H1KKR1_METEX Unreviewed; 341 AA.
AC H1KKR1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA-3-methyladenine glycosylase II {ECO:0000256|ARBA:ARBA00012000};
DE EC=3.2.2.21 {ECO:0000256|ARBA:ARBA00012000};
GN ORFNames=MetexDRAFT_3223 {ECO:0000313|EMBL:EHP91912.1};
OS Methylorubrum extorquens DSM 13060.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP91912.1, ECO:0000313|Proteomes:UP000004382};
RN [1] {ECO:0000313|EMBL:EHP91912.1, ECO:0000313|Proteomes:UP000004382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP91912.1,
RC ECO:0000313|Proteomes:UP000004382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., Pirttila A.,
RA Frank C., Woyke T.J.;
RT "The draft genome of Methylobacterium extorquens DSM 13060.";
RL Submitted (SEP-2011) 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 -!- 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:EHP91912.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGJK01000086; EHP91912.1; -; Genomic_DNA.
DR AlphaFoldDB; H1KKR1; -.
DR PATRIC; fig|882800.3.peg.3178; -.
DR Proteomes; UP000004382; Unassembled WGS sequence.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
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; 3.30.310.20; 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; 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.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:EHP91912.1};
KW Transferase {ECO:0000313|EMBL:EHP91912.1}.
FT DOMAIN 21..133
FT /note="DNA-3-methyladenine glycosylase AlkA N-terminal"
FT /evidence="ECO:0000259|SMART:SM01009"
FT DOMAIN 143..308
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 310..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 35513 MW; 3C9B6FBCDDC6BC0E CRC64;
MTGRERRLAG DTDMQPHATT VTRLPFRVPF DWDGVHAYLA ARAIPGVEIT CPGLYARSVA
SGGTHGIVRV QRASDDALAL TVVGPFHDAA TRAARLFDLG VDPDAVGTAL SADPFMAGLV
EARPGMRVPG AWDGFELAVR AILGQQVSVA AATRLAGKLV AAFGMPLTPG GAVAEPGLTH
VFPSPAALVD ADVALALNMP RARGAAIRAV AAAVLAEPDL FDPGQGLAVA VARLKALRGI
GDWTAHYVAM RALREADAMP TGDIGLLRAL EDEAGRPSAK ALEARSAAWR PWRAYAVLHL
WAHDAARTVA AGPTKTRPKT KTIPEQGAGC GHRAARAKVS P
//