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Database: UniProt
Entry: A0A0F7IF43_9EURY
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Original site: A0A0F7IF43_9EURY 
ID   A0A0F7IF43_9EURY        Unreviewed;      1145 AA.
AC   A0A0F7IF43;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=GAH_01023 {ECO:0000313|EMBL:AKG91653.1};
OS   Geoglobus ahangari.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Geoglobus.
OX   NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91653.1, ECO:0000313|Proteomes:UP000034723};
RN   [1] {ECO:0000313|EMBL:AKG91653.1, ECO:0000313|Proteomes:UP000034723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=234 {ECO:0000313|EMBL:AKG91653.1,
RC   ECO:0000313|Proteomes:UP000034723};
RA   Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA   Kashefi K.;
RT   "The complete genome sequence of the hyperthermophilic, obligate iron-
RT   reducing archaeon Geoglobus ahangari strain 234T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; CP011267; AKG91653.1; -; Genomic_DNA.
DR   RefSeq; WP_052747769.1; NZ_CP011267.1.
DR   AlphaFoldDB; A0A0F7IF43; -.
DR   STRING; 113653.GAH_01023; -.
DR   GeneID; 25419500; -.
DR   KEGG; gah:GAH_01023; -.
DR   HOGENOM; CLU_263797_0_0_2; -.
DR   InParanoid; A0A0F7IF43; -.
DR   OrthoDB; 45790at2157; -.
DR   Proteomes; UP000034723; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AKG91653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034723};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          678..792
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   DOMAIN          918..1015
FT                   /note="TaqI-like C-terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF12950"
SQ   SEQUENCE   1145 AA;  134927 MW;  A3D07033E3534878 CRC64;
     MPSKVEELRK EIEKKLSKFE MDEVTVGEKT YPLYVFDKDE DINLFEGFLY ANVNTKEEFS
     LLSNYKPPVS GYAGRIGIII YKDHEIYIKD YRTNKQIRKT ISKLNELFLK KLRKVLEEPK
     SENFSALFSR SDVIEEFYVL YKKSKEFLLD NINGISEEAK RKEFVDNFMM QMLTLWYLQE
     KGFFNRDKRY FITKFMDLKQ KKLFGGFESY YAFLRHFFKQ ISGYSDEPYV EDESIGKCVV
     IGPAVFLNGE DNPVIAIPDK CFYQEGVTEK LVNLTPKGRR RTISEDDIDF DIPLLNLFES
     RDWVDGDIDE YVLGSLYEKL MTEDKRKKTG AYYTPEEITS YICKNTIEPY LVDRINEEFG
     KDYGSIDELI NAGDKEGLTT LFNLLQNIKI LDPAVGSAHF LESAINVLVD IYRKLRDRAK
     EVGIEKLEIL VADEDGKIKP LNLLEIPEKE GLFEVYVKFF IILSRNIYGV DINPSALKVA
     RARLFLTLAR HFNVSAGVFI RFPNVHFNLR EGNSLIGYVD VPRGRKETTQ VTLDFNFEDH
     EIQYIREMIK VDDELKEYLP AIARSLRIEG DLVREVEEMN RILASKKIKW SEFEKVLKTK
     EKIIRVLVAS LNSKYAVKLN NLLREITKLF NRKLDEKFAE EYGIDLDKLK KLKDIPWERK
     MFHWVFEFPE VFLEKKGFDV VIGNPPYGRL KQIIEDKKEK DFMSKIYGKL YSYQVGNLNQ
     YKLFLERSYF LVSKGGYFSM IFPSSFLGEN DSKELRKLFF EKAMVKKILE FPERARVFEG
     ITQAVTILVY KKEIADQDYE FMLRTNIENR DMVATLSDFV NISRDDLKAL TGDEYRIPLF
     TNPKIEWEIL KHISKYPPFK GDENNPPIGD VGVGHLDETF DKEFMSDEPG DDLLIKGIHL
     DRYFVNLDPN GPKPRWIKNK EEFFRKKPEA KENIKFERII GRNTINKASK PRLRFAILKP
     GYVITNNVKF IILKDKNIYK FYLIALLNSK ILNWRFELFS FQNRVNNYEV EALPIPRIPL
     EDQKPFIILA KYMLFLKQYY NYFAKDDRHF QYIIDYFDNL IDCLVYELYL GDVVKIPIKP
     LVKDKLRDIE LPDNLLEEDK NKIEKTLNEI KEVFNTLEKD KELNENLYLM KLHPWIKQIY
     TSLGG
//
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