ID M0K2B5_9EURY Unreviewed; 1362 AA.
AC M0K2B5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=C435_14822 {ECO:0000313|EMBL:EMA14933.1};
OS Haloarcula californiae ATCC 33799.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662475 {ECO:0000313|EMBL:EMA14933.1, ECO:0000313|Proteomes:UP000011687};
RN [1] {ECO:0000313|EMBL:EMA14933.1, ECO:0000313|Proteomes:UP000011687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33799 {ECO:0000313|EMBL:EMA14933.1,
RC ECO:0000313|Proteomes:UP000011687};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:EMA14933.1}.
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DR EMBL; AOLS01000070; EMA14933.1; -; Genomic_DNA.
DR RefSeq; WP_007189717.1; NZ_AOLS01000070.1.
DR PATRIC; fig|662475.6.peg.2903; -.
DR Proteomes; UP000011687; Unassembled WGS sequence.
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; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF20473; MmeI_Mtase; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 522..610
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 778..875
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 976..1050
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
FT COILED 1317..1344
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1362 AA; 154225 MW; C9BBF552CE4550C1 CRC64;
MSQATLGSPY RNSDLFAGYY LDERVADLDD WECDDDAAQA FEDLQALWEG EGDLLPSYNE
DELLGAWIDE VLDILGFDTL QETTLPDSGG YNDRLLFESA DARRDAARQK RDGNTEGMYG
LSAAVLEAKQ WDADFTERFS EQRSYRDASH QIKYYLEHTP ERVAWGVLTN GKQWRLYGTK
DYATETYYEV NLPELLEEGD LEAFKYFYAF FWPEAFRETA GTSFLDTVWN ESETAAQELG
EDLQDNVFTA LRVLGEGFIH TNDLDIDPDD EDARAELKEQ SLVLLYRLMF VLYAESRGLI
HPDDPDAQDE YEEHFSLDQL RADIHEDIQS GDSFEDYSGH STRMWNRLEN LFGLVDEGEK
SLGIPPYNGG LFDEDQHEFL AENEVSDRHI AEVIYRLGTT EGDDGEFVLA DYADLDTRHL
GSIYEGLLEH EFRIAPEQYA AVAEDGGQVW KPATDVSVAD AVETVDQGEL YVVNDDGERK
ATGAYYTPDY VVSYIVEETV DPLLDDIKSE LEADGLEPSE TEYFRRFWQQ VLDLKILDPA
MGSAHFLTSA TGYLTEQVME VVREQEIQGY DEQELRREIA KECIYGVDVN GMAVELGKLS
MWLETLAADK PLAFLDHHLK TGNSLVGSDI TEVLSDDIEE NGGQLTLGQA FARARQQTLE
HVMDLMQDLL AIDNDELADI KSMEELYGEI REDPLYQRLF EVANVHTAEQ FGLDVPNGVY
EDMAGAIEDE REWAEIREAD WFSTAQAMAA DEDFFHWELE FPEVFFGADG SKLDGAGFDA
VIGNPPYVNI MRIPDKQVSY LSDTFDSAFR RFDLYVLFSE LAGDLIGNDG SYGYIVPDKI
LTESYASKWR QSILKEDSLT QILDLRDQNV FDDATNSPVV FILNSAAEAR SVTVDEHGPS
GTESRCELSL SEFRSLPESQ IRIDWHQETP AVLQSIRDGT FPLSRLFYAS WGTQPGNADR
FVFDEYPTDI EEGVTELIKG TDIDRYAIQY AGRYLWYDPD ELHRPAFPEL FENDKICLRK
VAGKRGLIAA LDRDSYYTED SVINLIRKSA LAEADDDILS ARGIEVVSEN RSSTNTENSK
TYDRDTTIYD DDLQLSKEVG LEPVLGIINS TLIHYYYSRA VSGQLNVFPE HVRRLPLEHD
QDVYQRLLKH VENVQSLTEQ RDALNCSLMD HLGSYSDGPT LADVGLTQPP EDSADSILQQ
TTEQKPNLRV GEASVVRESV STVEIQLTAR YKPDDEDAYE TDQWGYTETE PLPALRITDL
TETEGDLIEA FVPVAVDEAG GFAGFRETAT KTNSLVDRLR KLTLPAVDDV RDGLVSYMET
VERADELELK IERTDELIDE IVYELYGLTD EEIEIVEEAV GE
//
