ID C9N1Q5_9FUSO Unreviewed; 725 AA.
AC C9N1Q5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, 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=GCWU000323_02780 {ECO:0000313|EMBL:EEX73173.1};
OS Leptotrichia hofstadii F0254.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX73173.1, ECO:0000313|Proteomes:UP000006233};
RN [1] {ECO:0000313|EMBL:EEX73173.1, ECO:0000313|Proteomes:UP000006233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0254 {ECO:0000313|EMBL:EEX73173.1,
RC ECO:0000313|Proteomes:UP000006233};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX73173.1}.
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DR EMBL; ACVB02000032; EEX73173.1; -; Genomic_DNA.
DR RefSeq; WP_006806061.1; NZ_GG700634.1.
DR AlphaFoldDB; C9N1Q5; -.
DR STRING; 634994.GCWU000323_02780; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_012122_0_0_0; -.
DR Proteomes; UP000006233; 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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EEX73173.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006233};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..148
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 174..500
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 691..718
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 725 AA; 82720 MW; 65F6D17243791268 CRC64;
MESTYNALDY NKLISFIWSV ADDCLRDVYV RGKYRDVIIP MTVIRRFDAI IESKKTNIME
VKEMAETQGW DVAKTLDTAT GLPFYNTSNF CLKDLKYETN RQNLKRSFEE YLNGFSENIK
EILQKFDFNN QLTKMTDAGI LGSVIEKFTS SELNLSPYDE KNSYGEVIRK GLDNHAMGTL
FEEIIRKFNE ENNEEAGEHF TPRDVIELMA DIAMYPVMDK IKDGTYSIYD GACGTLGMGT
VAEERLKAFA KENSKEVSIH LIGQEVNPET YAISKADLLI KGGDTDSNNV YYGSTLSDDK
TSGQHFDFML SNPPYGKTWK TDLAILGSGN DKDPKKNITD RRFVRNYKEQ DDFRMIPDVS
DGQLLFLLNN ISKMKETEMG SRIVEVHNGS ALFTGDAGNG ASNARRFMIE KDLIEAIIQL
PENMFYNTGI TTYIWILSNR KEEKRKGKIQ LINASGIKTS LRKNMGKKNC EFSEDNRQFI
LKQYLNFEEN EYSKIFSNDE FGYYKVVVER PLRQAVLCDA NNIKEIEEEL EKIGVLSGAI
DKKVLAESFI KGTSSSMKEL EKSENVNTYL EVLKLMKSDE EYLNYAAFEK AFNKHLKKKD
IKGASLSKLA STGLLSRMIV KDEEAAIQKD SKGNVVADSE LRDTESIPMT FEGGIDEFIK
QEVLPYHADA FVDESKTQIG YEINFTKYFY KAKELESVEE IVNRIKELER QSDGMMASIL
EGLYE
//
