ID F7PKV9_9EURY Unreviewed; 1307 AA.
AC F7PKV9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HTIA_1979 {ECO:0000313|EMBL:CCQ34096.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:CCQ34096.1, ECO:0000313|Proteomes:UP000015381};
RN [1] {ECO:0000313|EMBL:CCQ34096.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(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}.
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DR EMBL; HF571520; CCQ34096.1; -; Genomic_DNA.
DR RefSeq; WP_008526559.1; NC_021921.1.
DR GeneID; 23799465; -.
DR KEGG; hti:HTIA_1979; -.
DR PATRIC; fig|1033806.12.peg.1966; -.
DR HOGENOM; CLU_265794_0_0_2; -.
DR OrthoDB; 237331at2157; -.
DR Proteomes; UP000015381; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; 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; IPR003356; DNA_methylase_A-5.
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; PF02384; N6_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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CCQ34096.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCQ34096.1}.
FT DOMAIN 391..459
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 704..811
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 1045..1129
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1307 AA; 150260 MW; 18ED1823301A7271 CRC64;
MADAAALHET LQAITERTDG EMSERDVENL FLEQGFYDAL DYRGTGTDLR SEFTLPDDRR
PDYLTLDNNE AVTAVYEFKT TGRELAPHED QLFHYMEYLR SEYGVLTNGE ELRLYQLGDD
RPMLTVSLAG VTESQARDLV SALQKREFDL RDPEDVSEFL ETLDPIPLDA EAELGQEHFF
DTFRLEEGSP FANLVTGLMD LLHELRDEQE AKFVKGAYDF WEATYADEPD EVPNSWEPFI
DGKQSLRDFM FCLESGHALL ARLLLAKATE DHDFFAGTGY EGMDDYFRGL QGFSQTINLD
AFPVAADNLI DDMQEQLVEG LFQDDIFVWW TDGYAEQLAR GHETGANQFQ KVAEGTGSIE
RISEATRDRF SRAVAEVFFN VLRFDFEEVE GDLLGDLYQR YFDPETRKAL GEFYTPQPVI
EYIMDGVGYE RGVSNERLID PACGSGTFLV EAVERYIEDI ERYEDDPDWE EHLRDLCTRP
RIVGLDIHPF AVLMAQIRFV VAILPAYREA KQKAERENRD FTLRRLPIYR TDTLRNEREL
TGADLGEDGA RQMTFDAMTE DEQDVRIPVP LPVEVDEDEA VETEDGFLVR RVRMPLFDTI
QLETGVNNFG EYFAALQGVL DTVKDHMALA EEFGGDFDWE YKSGLEERIN QHTSREYSGV
EEFFAPYVDD MLENVEYLKK EHNDGRLFKM FEDTVLALVV KNYMTYDYVV GNPPYVRVQN
LPDSQKEMME SLYDATTGNY DIYCPFYERG LDWLREDSGK LGFITPNQFM VTDYGEGLRE
VLLDEARIEE VYDFRDSGVF EDATNYPAIV ILDDEPDQAS REDNEIRCVR VKADTDEDRD
RELDTAIIES VREHRGEPGY SDEFIDVFDF PQGKLAADDY WAMMPPEELQ VFEKLEDEQD
AVIGDVTDAV FQGIRTSANK VYIVDVLDAD RVESDDSGET VTVVPTGESQ EYEIETDLLR
PFLEGDEVKR WRGDWGGLHV VHPYYAEETE DGELEAGLYS QDYLEENLPL TWDFFLAHKE
ELEGREGGRK EGKDDWYGYI YPKNLGKFEN PKIVQAHIAT DATFMIDEPG TWYFTTAYGV
LLTPQYRNLT EEMACQLNSK ALDFYFKHIT TVKMGGFYEY RSQYVEKLPC KTEDSAGVFG
TMREKAGGIV DTIDLDSKTD RFPEAYLGDY DGELDNVTYE WQTRRYPVSA DVQGDVDGNF
TVQAGRSDTI NDPAMYSDDR EARKQRAEYV HAAVDGRNVK SGEETTIPIP RSDEGVVELL
DRLDADREEV RETDIEALEA EIDEAVYDLF DLTEEEREVV EEYLEVF
//
