ID A0A1E7JVY7_9ACTN Unreviewed; 862 AA.
AC A0A1E7JVY7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AN216_23985 {ECO:0000313|EMBL:OEU94815.1};
OS Streptomyces oceani.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU94815.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEU94815.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU94815.1,
RC ECO:0000313|Proteomes:UP000176101};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEU94815.1}.
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DR EMBL; LJGU01000152; OEU94815.1; -; Genomic_DNA.
DR RefSeq; WP_070198788.1; NZ_LJGU01000152.1.
DR AlphaFoldDB; A0A1E7JVY7; -.
DR STRING; 1075402.AN216_23985; -.
DR PATRIC; fig|1075402.3.peg.1042; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000176101; 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 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; 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.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OEU94815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000176101};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..157
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 171..480
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 714..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97351 MW; B565CDC0C3E7D54D CRC64;
MAKLTLAQLE RHLWAAADIL RGTMDASEYK EYIFGLLFLK RANDEFEAAR EKVLEEARTE
LGLAGDLLEQ HLEEPSAYSE TGVLFVPKSA RWKLVSSGTQ NLNEERLRPA LQALEIQNPK
LKGLFDHLDF NRIGGSGASA STAKLANQRL RALIDHFGRI RLRTDDFEFP DLMGAAYEYL
IKEFADDAGR KGGEFYTPRA VVRMMVELLD PQQGSRIYDP CVGSGGMLIH AKEYVEERGG
DTSDMFFAGQ DANSGSWIMS TMNMVLHGVR SFSLTTGDTL TDPAHVPRSD EDRFHGVLSN
PPFSMDYSLA DLDHRAQRAE YGVTGERGKA DLMFLQHMLW ETKREKNPGM VITVMPHGVL
FRGGGEQEIR TKLLEEDVLE AVIGLAPNLF YGTGIPACIL VLRPPGTKVS KRQERVLFIN
ADQEYHAERA QNVLLPEHAE KIVSAFHAEN PEIPGFARLV SREKLRENGD NLNIRRYVDN
APPPEPQDVR AHLTGGMPRA EIEAKRGLLD AYGVKLADLF TEREPVDSDY VDFPSAERRP
DAARLAELAH PREEELQGAF TKWWEEEARH LEAVAATPER LADLLPSERK AGLMAVRGSL
MGSFVQRLGE VGLLDRHALS GAVAGWWYEA KYDLLALSEN GFGAVLDGWV DNVETMLAPE
QDPKTRKERK RSTAERRRAY DHKVVAAIAP DFLEELEAAD TRKAKLDARW KELNAKSEPA
DDDESGEESA DEQTGLTVDE LMELESLKKS RTKANAAVKR LENDFWFQRQ LTDQPQLGEE
EPRLFRARQE LDEEGERRVV LDLLRQDLAA KLEGHVVRRR RELVDAYGMW TDKYAVSLRE
IKRNVEFAEK QMKSRLKELG YE
//
