ID A0A0X7BFV8_9FLAO Unreviewed; 866 AA.
AC A0A0X7BFV8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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 ORFNames=AP058_00457 {ECO:0000313|EMBL:KVV16022.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV16022.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV16022.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV16022.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-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:KVV16022.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LLWK01000028; KVV16022.1; -; Genomic_DNA.
DR RefSeq; WP_066306441.1; NZ_LLWK01000028.1.
DR AlphaFoldDB; A0A0X7BFV8; -.
DR STRING; 1729581.AP058_00457; -.
DR PATRIC; fig|1729581.3.peg.487; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000059935; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KVV16022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059935};
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:KVV16022.1}.
FT DOMAIN 611..866
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 580..607
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 866 AA; 99336 MW; 97544A54554224C4 CRC64;
MAKVVYSNPV EVISFKIFGI FDAFRTNPKL SHLEDSVPVV LLLVSLYKDG VICEKTFTNN
FSLSDLKTLI FESNLDKETK DTYLLIFDVL SDSLSKVFSQ PLGYLNFHLF QNGKEMLSEN
FSNVIDDIIY KISKSQGRHA GEFIQPLELT RLMCGLANLS MNSKVFNPFA GLASFDIYLN
KNQEFFGQEL NKKTWALGAL RLMAYGKRVS SEYICEDSIL NWPKNTEKFD LIISNPPYGV
RFGNNYKGVE HEFRTIEQFL IKNGVDSLSE NGKLIVLLPQ GFLFRGMQEE RLRTLLIEED
LIDTIISLPG GLLLNTGIPL IILVLDRNKK LPGRVKFVDA KNFVNLKGPR EKVLNDQELL
SQIMDTSIID YSDNQNVVNE PSETYNSTSS AKINYLVRLV DNSQIKENDY NLSVTRYFQE
HIEGVKLRDI IEPYRGLRGN LPETGKLIRI RDLKDDNVNF LLDDKAVEET ELNRHMIHQI
DESCLLLAIR WKTLKPTFFE YKGSPIFKSQ DIFSAKIKQV KIDEVNIAYL INELQSEYVQ
KQLDSYRLGA TIPFIRQVDL LNVVIKLPSL EEQHAKVSGI IELSSKLKEL EVEKENLLKG
IKKEETESST SLSHILGKPL LSIGSSLEII QNTLSKVYPE WKDLLISETK QFYMIDAFES
ISKNVKYIQE LADENTALVS VYSFNLIEIN FLKFLSEFVK NEKKSLKNNI DIKLDIHEDI
KEQMNNKVFV FGNEQKLKIV LINLIDNAKN HAFIEPDMEN KINIEILPFT RNEREAYLLN
YDINGRKSYV EIRISNTGKP FPKDFTLEDY TRKNFAVGKT RNRGLGGYEV NEIIKAHNEG
KKALNISSSE DDKKYSSTVS FLIPII
//
