ID A0A0N0GLP2_9NEIS Unreviewed; 612 AA.
AC A0A0N0GLP2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:KPC50185.1};
GN ORFNames=WG78_18310 {ECO:0000313|EMBL:KPC50185.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC50185.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC50185.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC50185.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-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 -!- 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:KPC50185.1}.
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DR EMBL; LAQT01000031; KPC50185.1; -; Genomic_DNA.
DR RefSeq; WP_053939252.1; NZ_LAQT01000031.1.
DR AlphaFoldDB; A0A0N0GLP2; -.
DR STRING; 857265.WG78_18310; -.
DR REBASE; 133390; M.Aur41ORF18310P.
DR PATRIC; fig|857265.3.peg.3746; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000037939; Unassembled WGS sequence.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KPC50185.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037939};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPC50185.1}.
FT DOMAIN 6..138
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 152..453
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 612 AA; 68087 MW; C6ED3DEBEABF3167 CRC64;
MNHQALSSFI WSIADLLRGD YKRSDFGKVI LPFTVLRRLD CVLESTKPAV LAEFAARTQQ
GLKPDSFLTA KTQCPFYNTS PLDLTRLLGD QDNIRQNLYA YVQAFSPAAR DIFERFDFYA
QVERLAKAGL LYLVLKKFAN IDLHPDAVDN GQMGLAFEEL IRKFAEDSNE TAGEHFTPRE
VIRLMVNLLF IEDDDVLTPG NAVVRTLYDP TAGTGGMLSM AREYLLQHNP DARLTLFGQE
LNDESFAICK ADMLIKGQPV GNIVVGNTLS DDGHGARKFD YMLSNPPFGV EWKKVEKEVR
KEAADKGFAG RFGPGLPRVS DGSMLFLLHL ISKMRPAVDG GSRIGIVLNG SPLFTGGAGS
GESEIRRYVL ENDLVEAIIG LPADMFYNTG ISTYIWILSN KKPEDRKGWV QLIDGSSFWQ
KMRKSLGSKR KEMSDEHIAE ITRLFGDFAE ADQAIVLDAH GKEVSRSLML SGASAPIAPE
GGKVRVVPIS RVFRNQDFGY TTITVERPLR DEHGQIILGS KGKQKGKPQA DSALRDTENV
PLSDDIAAYF KREVQPHAPD AWIDEAKSKV GYEIPFNRHF YVFEPPRSLH TIDEELQTVS
ASIVKMLGGL AE
//