ID A0A1F0FUU9_9PORP Unreviewed; 810 AA.
AC A0A1F0FUU9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=HMPREF3027_06755 {ECO:0000313|EMBL:OFO52341.1};
OS Porphyromonas sp. HMSC077F02.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1739529 {ECO:0000313|EMBL:OFO52341.1, ECO:0000313|Proteomes:UP000178655};
RN [1] {ECO:0000313|Proteomes:UP000178655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC077F02 {ECO:0000313|Proteomes:UP000178655};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2016) 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 -!- 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:OFO52341.1}.
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DR EMBL; LTSX01000154; OFO52341.1; -; Genomic_DNA.
DR RefSeq; WP_070707749.1; NZ_KV820678.1.
DR AlphaFoldDB; A0A1F0FUU9; -.
DR STRING; 1739529.HMPREF3027_06755; -.
DR Proteomes; UP000178655; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029464; HSDR_N.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR Pfam; PF13588; HSDR_N_2; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000313|EMBL:OFO52341.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000178655};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:OFO52341.1}.
FT DOMAIN 21..128
FT /note="Type I restriction enzyme R protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13588"
FT DOMAIN 283..524
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 810 AA; 92319 MW; 388FD4064B759F03 CRC64;
MSIREWIKEN ISDYSKRIKT EEDVKVHIIL PYLKSLGYQI ENMRFENSMS VQAGTKSVTV
ISDIEIVENN NIEIVIDAKA PNISLNEKEI LQSISYAKLV STPPALYAVV TNGFDVITTN
IYTGKQTSEI PSRSELTRDV SRSRKRELSD IEIREVQSLM LTLNKPEELY AIIKESKDII
EKRGLIRSDQ SFKEMTKILL VKMNEERRAK NGDTNRFQID ILKRLAKADD TTPYEVFLNL
FSQAKQSYPI YTNPNEGINI SDEKCLLSVV EKLEPWSFLG TGDDIKGAVY EIFLKSTLRG
DFDQYFTPRE IVDFVVKFAN PNIGDKILDP ACGSGGFLIQ SFLYVTQKII NSPLSEVQRR
IIFEELIDKC LWGGEADEDL HVLAKINLIM HGDGYNNIYQ GDSLRNEKIL DNHFDLVLTN
PPFTIPYAFD DVLNQFELGI GRESQELDVL FVEKCVRSLK EDGELYIVLP EGLLNLPSYQ
YFREWIMSKC YITLSIGLPE GAFIPFGKSV SKTAILGLRK RNLSNDNKPE YVFLGTVSAV
GYEVGKSTYK PIEYNDLLEF TFSQSSGVFQ DIRTTKSGGE YVWLKQENVT SYRIDSQYLI
NSVDIKAIHT KFSNLQRLDK VCSIENNSIK PLAEQEYYYL EIPDVSPDTG TISNIRKLKG
DEIGDSFNLA KGGDIAYTRI NPRLNRVFII PDEIEEVLIS KEAYVLSLHN ESMIISNYVL
AAILQSELVK SQLIRIATGS SSSRARIQQD AFLNSVFIPI PDLATQRKIH RNMSKAYNDY
WEASQKFLKN YTECQKALLT DIDINNIRKA
//
